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Enzyme Nomenclature
Information on EC 3.6.3.50 - protein-secreting ATPase
for references in articles please use BRENDA:EC3.6.3.50
Word Map on EC 3.6.3.50
- 3.6.3.50
- agrobacterium
- tumefaciens
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virb10
- campylobacter
- jejuni
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injectisome
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cytolethal
- biotechnology
- drug development
- medicine
- pharmacology
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
3.6.3.50
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RECOMMENDED NAME
GeneOntology No.
protein-secreting ATPase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
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ATP + H2O = ADP + phosphate
analysis of protein-protein interactions of type III secretion apparatus, direct interactions between chaperone, effector, and type III component, model of translocation
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ATP + H2O = ADP + phosphate
model of domain construction and complex of subunits
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ATP + H2O = ADP + phosphate
isolation of intermediate export complex containing chaperone, substrate, FliI ATPase and regulator FliH, complex of chaperone and substrate is required for interaction with ATPase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (protein-secreting)
A non-phosphorylated, non-ABC (ATP-binding cassette) ATPase that is involved in protein transport. There are several families of enzymes included here, e.g. ATP-hydrolysing enzymes of the general secretory pathway (Sec or Type II), of the virulence-related secretory pathway (Type III) and of the conjugal DNA-protein transfer pathway (Type IV). Type II enzymes occur in bacteria, archaea and eucarya, whereas type III and type IV enzymes occur in bacteria where they form components of a multi-subunit complex.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enterohemoraghic strain and enteropathogenic strain; type III secretion system
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two type III secretion systems, which are encoded by two distinct gene clusters termed SPI-1 and SPI-2; type III secretion system
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wild-type strain W22703 and strain EC2 DELTA(yscM1 yscM2), gene yscP
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
enzyme FliI is a member of the Walker-type ATPase family
evolution
A0A0C6EWK5
phylogenetic analysis and tree of T3SS ATPases, overview
evolution
VirB11 belongs to the superfamily of traffic ATPases, which includes members of the type II secretion system and the type IV pilus and archaeal flagellar assembly apparatus
evolution
the enzyme contains a two-helix-finger motif at the entrance of the modeled central pore of the InvC hexamer. The motif is highly conserved among type III secretion-associated ATPases, including those associated with the flagellar assembly apparatus. In addition to the tyrosine residue (Tyr385 in InvC) located at the center of the loop, other residues within the loop are highly conserved, such as Gly383, Glu384, and Gly388. Similarities between type III secretion ATPases and other ATP-driven protein translocases/unfoldases
evolution
the T2SS secretion ATPase GspE belongs to the family of Type II/IV secretion ATPases
evolution
Agrobacterium tumefaciens C58 / ATCC 33970
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VirB11 belongs to the superfamily of traffic ATPases, which includes members of the type II secretion system and the type IV pilus and archaeal flagellar assembly apparatus
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evolution
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the enzyme contains a two-helix-finger motif at the entrance of the modeled central pore of the InvC hexamer. The motif is highly conserved among type III secretion-associated ATPases, including those associated with the flagellar assembly apparatus. In addition to the tyrosine residue (Tyr385 in InvC) located at the center of the loop, other residues within the loop are highly conserved, such as Gly383, Glu384, and Gly388. Similarities between type III secretion ATPases and other ATP-driven protein translocases/unfoldases
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malfunction
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abrogation of the interaction between the CesABEspA complex and EscN resulted in severe secretion and infection defects
malfunction
loss of enzyme BsaS function either via direct genetic inactivation or treatment with the inhibitor compound 939 results in increased susceptibility of Burkholderia pseudomallei to microtubule-associated protein light chain 3-associated phagocytosis in infected RAW 264.7 cells, leading to elevated levels of intracellular killing. The bsaS deletion mutant is highly attenuated for virulence in BALB/c mice
malfunction
secretion of glyceraldehyde-3-phosphate dehydrogenase is abolished in mutants defective in the type III ATPase EscN. Complementation with escN gene restores GAPDH secretion
malfunction
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loss of enzyme BsaS function either via direct genetic inactivation or treatment with the inhibitor compound 939 results in increased susceptibility of Burkholderia pseudomallei to microtubule-associated protein light chain 3-associated phagocytosis in infected RAW 264.7 cells, leading to elevated levels of intracellular killing. The bsaS deletion mutant is highly attenuated for virulence in BALB/c mice
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metabolism
enteropathogenic (EPEC) Escherichia coli secrete GAPDH through a type III secretion system into the culture medium. GAPDH secretion is not linked to outer membrane vesicles and depends on growth conditions. The secretion process is often dependent on a bacterial chaperone. The chaperone CesT displays broad substrate specificity and plays a central role in the recruitment of multiple type III effectors to the T3SS apparatus
metabolism
A0A0C6EWK5
the enzyme is an ATPase enzyme involved in the type III secretion system, T3SS
metabolism
the enzyme is part of the type II secretion system (T2SS), which is present in many Gram-negative bacteria and is responsible for secreting a large number of folded proteins, including major virulence factors, across the outer membrane
metabolism
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pathogenicity of many Gram-negative bacteria depends on a type III secretion (T3S) system which translocates bacterial effector proteins into eukaryotic cells. The membrane-spanning secretion apparatus is associated with a cytoplasmic ATPase complex and a predicted cytoplasmic (C) ring structure which is proposed to provide a substrate docking platform for secreted proteins. The putative C ring component HrcQ from the plant pathogenic bacterium Xanthomonas campestris pv. vesicatoria is essential for bacterial pathogenicity and type III secretion system, overview. The general substrate acceptor site of the T3S system, HrcQ, localizes to the cytoplasm and associates with the bacterial membranes under type III secretion system-permissive conditions binding to the cytoplasmic T3S-ATPase HrcN, its predicted regulator HrcL and the cytoplasmic domains of the inner membrane proteins HrcV and HrcU. HpaB presumably targets effector proteins to the ATPase HrcN of the T3S system which can dissociate HpaB-effector protein complexes and thus might facilitate the entry of effector proteins into the inner channel of the T3S system
metabolism
Gram-negative bacteria use the type II secretion (T2S) system to secrete exoproteins for attacking animal or plant cells or to obtain nutrients from the environment. The system is unique in helping folded proteins traverse the outer membrane. The secretion machine comprises multiple proteins spanning the cell envelope and a cytoplasmic ATPase. Activity of the ATPase, when copurified with the cytoplasmic domain of an interactive ATPase partner, is stimulated by an acidic phospholipid, suggesting the membrane-associated ATPase is actively engaged in secretion
metabolism
type III secretion system T3SS-1 facilitates host cell invasion and inflammation, whereas type III secretion system T3SS-2 mediates intracellular survival and immune evasion
metabolism
type III secretion systems (T3SS) are a primary mechanism employed by Chlamydia to interact with the eukaryotic host cell, enabling access to the intracellular environment, modification of the early endosome and to establish and maintain an intracellular environment. T3SSs are a critical component of two bacterial systems: the flagellum, an extracellular motor essential to motility,4,5 and the non-flagellar (NF)-T3SS, an energy-dependent, molecular syringe that facilitates the transport of host-altering effector proteins into the host cytosol during infection; type III secretion systems (T3SS) are a primary mechanism employed by Chlamydia to interact with the eukaryotic host cell, enabling access to the intracellular environment, modification of the early endosome and to establish and maintain an intracellular environment. T3SSs are a critical component of two bacterial systems: the flagellum, an extracellular motor essential to motility,4,5 and the non-flagellar (NF)-T3SS, an energy-dependent, molecular syringe that facilitates the transport of host-altering effector proteins into the host cytosol during infection
metabolism
the type II secretion system (T2SS), a multiprotein machinery spanning two membranes in Gram-negative bacteria, incudes the critical multidomain GspEEpsE, and is responsible for the secretion of folded proteins from the periplasm across the outer membrane
metabolism
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type III secretion systems (T3SS) are a primary mechanism employed by Chlamydia to interact with the eukaryotic host cell, enabling access to the intracellular environment, modification of the early endosome and to establish and maintain an intracellular environment. T3SSs are a critical component of two bacterial systems: the flagellum, an extracellular motor essential to motility,4,5 and the non-flagellar (NF)-T3SS, an energy-dependent, molecular syringe that facilitates the transport of host-altering effector proteins into the host cytosol during infection; type III secretion systems (T3SS) are a primary mechanism employed by Chlamydia to interact with the eukaryotic host cell, enabling access to the intracellular environment, modification of the early endosome and to establish and maintain an intracellular environment. T3SSs are a critical component of two bacterial systems: the flagellum, an extracellular motor essential to motility,4,5 and the non-flagellar (NF)-T3SS, an energy-dependent, molecular syringe that facilitates the transport of host-altering effector proteins into the host cytosol during infection
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metabolism
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type III secretion system T3SS-1 facilitates host cell invasion and inflammation, whereas type III secretion system T3SS-2 mediates intracellular survival and immune evasion
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metabolism
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pathogenicity of many Gram-negative bacteria depends on a type III secretion (T3S) system which translocates bacterial effector proteins into eukaryotic cells. The membrane-spanning secretion apparatus is associated with a cytoplasmic ATPase complex and a predicted cytoplasmic (C) ring structure which is proposed to provide a substrate docking platform for secreted proteins. The putative C ring component HrcQ from the plant pathogenic bacterium Xanthomonas campestris pv. vesicatoria is essential for bacterial pathogenicity and type III secretion system, overview. The general substrate acceptor site of the T3S system, HrcQ, localizes to the cytoplasm and associates with the bacterial membranes under type III secretion system-permissive conditions binding to the cytoplasmic T3S-ATPase HrcN, its predicted regulator HrcL and the cytoplasmic domains of the inner membrane proteins HrcV and HrcU. HpaB presumably targets effector proteins to the ATPase HrcN of the T3S system which can dissociate HpaB-effector protein complexes and thus might facilitate the entry of effector proteins into the inner channel of the T3S system
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physiological function
Q9Z748
the N-terminal domain of ATPase FliI interacts with the cytoplasmic domain of falgellar ortholog FlhA, but not with FliF. The FlhA binding domain resides in the N-terminal 150 amino acids of FliI. FliI also interacts with flagellar proteins CdsL and CopN
physiological function
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interaction of ATPase InvC with type III secretion effector SopD. SopD helix II region, residues 268-302, is essential for the interaction with InvC
physiological function
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deletion of the catalytic domain of the yscN gene in Yersinia pestis CO92 attenuated the strain over three million-fold in the Swiss-Webster mouse model of bubonic plague
physiological function
the flagellar type III export apparatus consists of a proton-driven export gate and an ATPase complex. The export process is well regulated by dynamic, specific and cooperative interactions among export components, chaperones, and export substrates in a timely manner
physiological function
the flagellar type III export apparatus consists of a proton-driven export gate and an ATPase complex. The export process is well regulated by dynamic, specific and cooperative interactions among export components, chaperones, and export substrates in a timely manner. Chaperone FliD binds to FliI and significantly enhances or stabilizes the weak interaction between the C-terminal ATPase domain FliICAT and flagellar chaperone FliT94 presumably through cooperative interactions among FliICAT, FliD and FliT94. Because FliH suppresses ATP hydrolysis by FliI, FliH coordinates ATP hydrolysis by FliI with protein export
physiological function
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the enzyme is the key protein in the type III secretion (TTS) system, a multi-protein machinery that has evolved to deliver bacterial virulence proteins directly into eukaryotic cells, through an organelle termed the injectisome. The ATPase EscN is a peripheral membrane protein located at the entrance of the injectisome, at the cytoplasmic base of the injectisome, and forms a ring structure. Enzyme EscN selectively engages the EspA-loaded CesAB, but not the unliganded CesAB. The targeting signal is encoded in a disorder-order structural transition in CesAB that is elicited only upon binding of its physiological substrate, EspA. There is no interaction between CesAB and EscN, CesAB appears not to be engaged by the injectisome ATPase in its substrate-free form, but the CesABEspA heterodimer interacts specifically with the EscN ATPase mediated by CesAB. Efficient targeting of CesAB-EspA to ATPase EscN is required for EspA secretion
physiological function
a two-helix-finger motif and a conserved loop located at the entrance of and within the predicted pore formed by the hexameric ATPase are essential for the ATP-driven protein translocase InvC function in the type III secretion system. Type III secretion machines are essential for the virulence or symbiotic relationships of many bacteria. An essential component of these machines is a highly conserved ATPase, which is necessary for the recognition and secretion of proteins destined to be delivered by the type III secretion pathway, e.g. secretion of the regulatory protein InvJ (early substrate), the translocases SipB, SipC, and SipD (middle substrate), and the effector proteins SptP and SopB (late substrates)
physiological function
Gram-negative pathogens utilize type III secretion systems (T3SSs) to inject bacterial effector proteins into the host. An important component of T3SSs is a conserved ATPase that captures chaperone-effector complexes and energizes their dissociation to facilitate effector translocation. Chaperones engage type III secretion system ATPases to facilitate effector secretion, molecular basis of the chaperone-T3SS ATPase interaction interface, modeling of the interaction between the multicargo chaperone, SrcA, and the enzyme SsaN, overview. Importance of the chaperone-T3SS ATPase interaction for the pathogenesis of Salmonella
physiological function
among the many protein components of the T2SS, the secretion ATPase GspE plays an essential role, and is likely responsible for providing energy for the protein translocation process
physiological function
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HrcQ interacts with conserved components of the type-III secretion system at the inner membrane including the inner membrane proteins HrcV and HrcU, the ATPase HrcN and its predicted regulator HrcL
physiological function
the enzyme ATPase foci colocalizes with the secretion channel. The ATPase may be transiently associated with the T2S machine by alternating between a cytoplasmic and a machine-associated state in a secretion-dependent manner, terminating the ATPase activity when secretion is completed. Function-related dynamic assembly may be the essence of the T2S machine, overview. The T2S ATPase acts as a transiently associated part of the secretion machine
physiological function
the enzyme YsaN is negatively regulated by YsaL, overview
physiological function
enzyme SsaN hydrolyzes ATP in vitro and is essential for type III secretion system, T3SS, function and Salmonella virulence in vivo. Protein-protein interaction analyses reveal that SsaN interacts with SsaK and SsaQ to form the C ring complex. The T3SS-2-associated ATPase SsaN contributes to T3SS-2 effector translocation efficiency. Enzyme SsaN is required for the export of another T3SS-2 effector, SseJ, which is encoded outside of the T3SS-2 region. Enzyme SsaN releases the translocator protein SseB from the T3SS-2 specific chaperone SsaE in an ATP-dependent manner. Gene ssaN contributes to Salmonella virulence in the mouse model of systemic infection
physiological function
proper recognition, unfolding, and secretion of substrates in both type III secretion systems are regulated by interactions between the T3SS ATPase and ATPase-regulator proteins, presence of both flagellar and NF-T3SS ATPase/ATPase-regulator pairs in Chlamydia; proper recognition, unfolding, and secretion of substrates in both type III secretion systems are regulated by interactions between the T3SS ATPase and ATPase-regulator proteins, presence of both flagellar and NF-T3SS ATPase/ATPase-regulator pairs in Chlamydia, interactions between the flagellar ATPase (FliI) and the NF-T3SS ATPase regulator (CdsL)
physiological function
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proper recognition, unfolding, and secretion of substrates in both type III secretion systems are regulated by interactions between the T3SS ATPase and ATPase-regulator proteins, presence of both flagellar and NF-T3SS ATPase/ATPase-regulator pairs in Chlamydia; proper recognition, unfolding, and secretion of substrates in both type III secretion systems are regulated by interactions between the T3SS ATPase and ATPase-regulator proteins, presence of both flagellar and NF-T3SS ATPase/ATPase-regulator pairs in Chlamydia, interactions between the flagellar ATPase (FliI) and the NF-T3SS ATPase regulator (CdsL)
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physiological function
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a two-helix-finger motif and a conserved loop located at the entrance of and within the predicted pore formed by the hexameric ATPase are essential for the ATP-driven protein translocase InvC function in the type III secretion system. Type III secretion machines are essential for the virulence or symbiotic relationships of many bacteria. An essential component of these machines is a highly conserved ATPase, which is necessary for the recognition and secretion of proteins destined to be delivered by the type III secretion pathway, e.g. secretion of the regulatory protein InvJ (early substrate), the translocases SipB, SipC, and SipD (middle substrate), and the effector proteins SptP and SopB (late substrates); enzyme SsaN hydrolyzes ATP in vitro and is essential for type III secretion system, T3SS, function and Salmonella virulence in vivo. Protein-protein interaction analyses reveal that SsaN interacts with SsaK and SsaQ to form the C ring complex. The T3SS-2-associated ATPase SsaN contributes to T3SS-2 effector translocation efficiency. Enzyme SsaN is required for the export of another T3SS-2 effector, SseJ, which is encoded outside of the T3SS-2 region. Enzyme SsaN releases the translocator protein SseB from the T3SS-2 specific chaperone SsaE in an ATP-dependent manner. Gene ssaN contributes to Salmonella virulence in the mouse model of systemic infection
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physiological function
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HrcQ interacts with conserved components of the type-III secretion system at the inner membrane including the inner membrane proteins HrcV and HrcU, the ATPase HrcN and its predicted regulator HrcL
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additional information
flagellar type III export apparatus structure analysis, structure-function relationship, overview. Because FliI binds to FlhAC and the C-terminal domain of FlhB (FlhBC), the FliI6-FliJ ring complex is formed on the FlhAC-FlhBC platform and is stably anchored to the platform through the interaction between FliHEN and FlhATM
additional information
flagellar type III export apparatus structure analysis, structure-function relationship, overview. Because FliI binds to FlhAC and the C-terminal domain of FlhB (FlhBC), the FliI6-FliJ ring complex is formed on the FlhAC-FlhBC platform and is stably anchored to the platform through the interaction between FliHEN and FlhATM
additional information
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a recombinant well folded CesAB D14L/R18D/E20L mutant homodimer variant binds specifically to EscN in contrast to the monomeric form
additional information
A0A0C6EWK5
molecular docking studies and protein-protein interaction network of pscN ATPase, overview
additional information
structure-function relationship, modeling based on the crystal structures of EscN, a T3SS ATPase from enteropathogenic Escherichia coli, PDB IDs 2OBM and 2OBL, and a crystal structure of the F1 ATPase hexamer, PDB ID 1BMF, overview. K165 is the catalytic residue of the ATPase
additional information
enzyme structure molecular modeling, overview
additional information
the conserved arginine residue at position 192 of SsaN located in the dicyclohexylcarbodiimide-binding site (DCCD box) in the catalytic domain is essential for ATPase activity
additional information
protein-protein interactions involving CT398, RpoN, and both flagellar and non-flagellar T3SS ATPase and ATPase regulators, overview. CT398 functions as a regulatory protein partner in several key areas of chlamydial biology, including as a posttranslational chaperone of RpoN and as a modulator of T3S-dependent events, CT398 protein structure analysis, detailed overview; protein-protein interactions involving CT398, RpoN, and both flagellar and non-flagellar T3SS ATPase and ATPase regulators, overview. CT398 functions as a regulatory protein partner in several key areas of chlamydial biology, including as a posttranslational chaperone of RpoN and as a modulator of T3S-dependent events, CT398 protein structure analysis, detailed overview
additional information
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protein-protein interactions involving CT398, RpoN, and both flagellar and non-flagellar T3SS ATPase and ATPase regulators, overview. CT398 functions as a regulatory protein partner in several key areas of chlamydial biology, including as a posttranslational chaperone of RpoN and as a modulator of T3S-dependent events, CT398 protein structure analysis, detailed overview; protein-protein interactions involving CT398, RpoN, and both flagellar and non-flagellar T3SS ATPase and ATPase regulators, overview. CT398 functions as a regulatory protein partner in several key areas of chlamydial biology, including as a posttranslational chaperone of RpoN and as a modulator of T3S-dependent events, CT398 protein structure analysis, detailed overview
additional information
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protein-protein interactions involving CT398, RpoN, and both flagellar and non-flagellar T3SS ATPase and ATPase regulators, overview. CT398 functions as a regulatory protein partner in several key areas of chlamydial biology, including as a posttranslational chaperone of RpoN and as a modulator of T3S-dependent events, CT398 protein structure analysis, detailed overview; protein-protein interactions involving CT398, RpoN, and both flagellar and non-flagellar T3SS ATPase and ATPase regulators, overview. CT398 functions as a regulatory protein partner in several key areas of chlamydial biology, including as a posttranslational chaperone of RpoN and as a modulator of T3S-dependent events, CT398 protein structure analysis, detailed overview
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additional information
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structure-function relationship, modeling based on the crystal structures of EscN, a T3SS ATPase from enteropathogenic Escherichia coli, PDB IDs 2OBM and 2OBL, and a crystal structure of the F1 ATPase hexamer, PDB ID 1BMF, overview. K165 is the catalytic residue of the ATPase; the conserved arginine residue at position 192 of SsaN located in the dicyclohexylcarbodiimide-binding site (DCCD box) in the catalytic domain is essential for ATPase activity
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
HopB1/in + ATP + H2O
HopB1/out + ADP + phosphate
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intrinsic protein substrate, type II effector of pathogen
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-
?
HopPtoN/in + ATP + H2O
HopPtoN/out + ADP + phosphate
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Hrp outer protein effector of pathogen, that is translocated into host cells in enzyme-dependent secretion
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-
?
HrpJ/in + ATP + H2O
HrpJ/out + ADP + phosphate
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intrinsic protein substrate, its secretion is required for pathogenicity and translocation of effectors into plant cells
-
-
?
HrpK/in + ATP + H2O
HrpK/out + ADP + phosphate
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intrinsic protein substrate, C-terminal half of protein is required for translocation
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-
?
YopR/in + ATP + H2O
YopR/out + ADP + phosphate
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eleven N-terminal amino acids of YopR sectretion substrate function as secretion signal required for binding to enzyme
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-
?
ATP + H2O
ADP + phosphate
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secretion of amylase and protease
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?
ATP + H2O
ADP + phosphate
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a signature of the sec-dependent protein transport, by the type II and the type IV secretion, is the presence of a short, about 30 amino acids, mainly hydrophobic amino-terminal signal sequence in the exported protein. The signal sequence aids protein export and is cleaved off by a periplasmic signal peptidase when the exported protein reaches the periplasm
-
?
ATP + H2O
ADP + phosphate
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type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
-
ATP + H2O
ADP + phosphate
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type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
a signature of the sec-dependent protein transport, by the type II and the type IV secretion, is the presence of a short, about 30 amino acids, mainly hydrophobic amino-terminal signal sequence in the exported protein. The signal sequence aids protein export and is cleaved off by a periplasmic signal peptidase when the exported protein reaches the periplasm
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?
ATP + H2O
ADP + phosphate
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type II protein secretion system exports flagellar subunits across the cytoplasmic membrane
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?
ATP + H2O
ADP + phosphate
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the type III secretion system is dependent on ATPase activity, which catalyzes the unfolding of proteins and the secretion of effector proteins through the injectisome. CdsN, Cpn0707, is the T3S ATPase. CdsN interacts with CdsD, CdsL, CdsQ, and CopN, four putative structural components of the T3S system, CdsN also interacts with an unannotated protein, Cpn0706, a putative CdsN chaperone, overview
-
-
?
ATP + H2O
ADP + phosphate
Chlamydia pneumoniae CWL-029 / ATCC VR1310
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the type III secretion system is dependent on ATPase activity, which catalyzes the unfolding of proteins and the secretion of effector proteins through the injectisome. CdsN, Cpn0707, is the T3S ATPase. CdsN interacts with CdsD, CdsL, CdsQ, and CopN, four putative structural components of the T3S system, CdsN also interacts with an unannotated protein, Cpn0706, a putative CdsN chaperone, overview
-
-
?
ATP + H2O
ADP + phosphate
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type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
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secretion of pectate lyase and a cellulase through a type II secretion machinery, the Out system
-
?
ATP + H2O
ADP + phosphate
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the cloned Erwinia chrysanthemi Hrp type III protein secretion system functions in Escherichia coli to deliver Pseudomonas syringae Avr signals to plant cells and to secrete Avr proteins in culture
-
?
ATP + H2O
ADP + phosphate
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type II enzyme system: secretion of a large number of enzymes, including cellulases and pectinases
-
?
ATP + H2O
ADP + phosphate
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in addition the protein binds DNA and interacts with PcfF and PcfG
-
-
ir
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
-
ATP + H2O
ADP + phosphate
-
secretion of pectic enzymes and cellulase by the type II secretion system
-
-
-
ATP + H2O
ADP + phosphate
-
secretion of pectic enzymes and cellulase by the type II secretion system
-
?
ATP + H2O
ADP + phosphate
-
a signature of the sec-dependent protein transport, by the type II and the type IV secretion, is the presence of a short, about 30 amino acids, mainly hydrophobic amino-terminal signal sequence in the exported protein. The signal sequence aids protein export and is cleaved off by a periplasmic signal peptidase when the exported protein reaches the periplasm
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
-
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
-
ATP + H2O
ADP + phosphate
-
a signature of the sec-dependent protein transport, by the type II and the type IV secretion, is the presence of a short, about 30 amino acids, mainly hydrophobic amino-terminal signal sequence in the exported protein. The signal sequence aids protein export and is cleaved off by a periplasmic signal peptidase when the exported protein reaches the periplasm
-
?
ATP + H2O
ADP + phosphate
-
PilB and PilT of the type IV pili, T4P, system in Myxococcus xanthus have ATPase activity acting at distinct steps in the T4P extension/retraction cycle in vivo
-
-
?
ATP + H2O
ADP + phosphate
-
PilB and PilT of the type IV pili, T4P, system in Myxococcus xanthus have ATPase activity in vitro
-
-
?
ATP + H2O
ADP + phosphate
-
PilB and PilT of the type IV pili, T4P, system in Myxococcus xanthus have ATPase activity acting at distinct steps in the T4P extension/retraction cycle in vivo
-
-
?
ATP + H2O
ADP + phosphate
-
PilB and PilT of the type IV pili, T4P, system in Myxococcus xanthus have ATPase activity in vitro
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
type II secretion apparatus is required for secretion of pectate lyase and cellulase
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system is required for secretion of pectinase and cellulase
-
-
-
ATP + H2O
ADP + phosphate
-
type II enzyme: exports the largest number of proteins from this organism, including lipase, phospholipase C, alkaline phosphatase, exotoxin A, elastase and LasA. At least two different secretins are able to function in type II secretion: XcpQ and XqhA
-
?
ATP + H2O
ADP + phosphate
-
secretion of elastase, exotoxin A, phospholipase C, and other proteins
-
-
-
ATP + H2O
ADP + phosphate
-
secretion of elastase, exotoxin A, phospholipase C, and other proteins
-
?
ATP + H2O
ADP + phosphate
-
a signature of the sec-dependent protein transport, by the type II and the type IV secretion, is the presence of a short, about 30 amino acids, mainly hydrophobic amino-terminal signal sequence in the exported protein. The signal sequence aids protein export and is cleaved off by a periplasmic signal peptidase when the exported protein reaches the periplasm
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
-
ATP + H2O
ADP + phosphate
-
the enzyme shows requirement for three invariant acidic residues in the Walker Asp Box motif, and for two invariant His residues in the His Box motif, structure-function analysis and modelling, overview. The Walker A motif is involved in ATP binding, while the Walker B motif is involved in the hydrolysis of ATP
-
-
?
ATP + H2O
ADP + phosphate
-
the enzyme shows requirement for three invariant acidic residues in the Walker Asp Box motif, and for two invariant His residues in the His Box motif, structure-function analysis and modelling, overview. The Walker A motif is involved in ATP binding, while the Walker B motif is involved in the hydrolysis of ATP
-
-
?
ATP + H2O
ADP + phosphate
-
the Hrp type III protein secretion system catalyzes the Hrp pilus assembly
-
-
-
ATP + H2O
ADP + phosphate
-
the Hrp type III protein secretion system catalyzes the Hrp pilus assembly
-
?
ATP + H2O
ADP + phosphate
-
plays a key role in secretion of the virulence proteins HrpW and AvrPto
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
secretion of the avirulence proteins HrmA and AvrPto from Pseudomonas syringae pathovars
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
FliH regulates the activity of the FliI ATPase and binds to FliI suppressing its oligomerization and ATPase activity. At the level of the export ATPase complex, two activities have been reported for FliJ, i.e. a T3SS chaperone escort activity and a stimulation of the FliI ATPase activity
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
FliI, an ATPase, provides the energy for export of the protein subunits, that form the filament and other structures to outside the membrane, via a specialized secretion apparatus, overview. This apparatus is related to the injectisome used by many gram-negative pathogens and symbionts to transfer effector proteins into host cells by type III secretion mechanism. Flagellar secretion in Salmonella enterica requires the proton motive force and does not require ATP hydrolysis by FliI. FliI is non-essential for flagellar assembly and function
-
-
?
ATP + H2O
ADP + phosphate
malachite green reagent assay for activity determination
-
-
?
ATP + H2O
ADP + phosphate
malachite green reagent assay for activity determination
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
type III protein-secretion system delivers bacterial proteins into host cells that mediate this bacterium“s ability to enter nonpathogenic cells
-
-
-
ATP + H2O
ADP + phosphate
-
type III protein-secretion system delivers bacterial proteins into host cells that mediate this bacterium“s ability to enter nonpathogenic cells
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
the two type II secretion systems, SPI-1 and SPI-2 appear to play different roles during pathogenesis, with SPI-1 being required for initial penetration of the intestinal mucosa and SPI-2 necessary for subsequent systemic stages of infection
-
-
-
ATP + H2O
ADP + phosphate
-
FliI, the ATPase involved in bacterial flagellar protein export, forms a complex with its regulator FliH in the cytoplasm and hexamerizes upon docking to the export gate composed of integral membrane proteins
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
FliI, the ATPase involved in bacterial flagellar protein export, forms a complex with its regulator FliH in the cytoplasm and hexamerizes upon docking to the export gate composed of integral membrane proteins
-
-
?
ATP + H2O
ADP + phosphate
-
type III protein-secretion system delivers bacterial proteins into host cells that mediate this bacterium“s ability to enter nonpathogenic cells
-
-
-
ATP + H2O
ADP + phosphate
-
type III protein-secretion system delivers bacterial proteins into host cells that mediate this bacterium“s ability to enter nonpathogenic cells
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
pathogens use the type III system as a key virulence mechanism
-
-
-
ATP + H2O
ADP + phosphate
-
invasion of epithelial cells by Shigella flexneri is mediated by a set of translocated bacterial invasins, the Ipa proteins, and its dedicated type III secretion system, Mxi-Spa
-
-
?
ATP + H2O
ADP + phosphate
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
-
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
secretion of AvrBs2 to pepper plants
-
-
-
ATP + H2O
ADP + phosphate
-
secretion of AvrBs2 to pepper plants
-
?
ATP + H2O
ADP + phosphate
-
a signature of the sec-dependent protein transport, by the type II and the type IV secretion, is the presence of a short, about 30 amino acids, mainly hydrophobic amino-terminal signal sequence in the exported protein. The signal sequence aids protein export and is cleaved off by a periplasmic signal peptidase when the exported protein reaches the periplasm
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
-
ATP + H2O
ADP + phosphate
-
The membrane-spanning type III secretion, T3S, system injects effector proteins into the cytosol of eukaryotic host cells, the T3S apparatus is associated with an ATPase that presumably provides the energy for the secretion process. HrcN is crucial for effector protein translocation and is essential for T3S and bacterial pathogenicity
-
-
?
ATP + H2O
ADP + phosphate
-
XpsE is the key component of the multi-protein complex of the type II secretion system T2SS, comprising 12 protein components, regulation occurs via Clp, a homologue of the cyclic AMP-receptor protein, by directly binding to the xpsE promoter region, overview
-
-
?
ATP + H2O
ADP + phosphate
-
XpsE possesses a nucleotide-binding Walker A motif involved in ATP binding
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
Yersinia enterolytica
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
-
ATP + H2O
ADP + phosphate
-
the ATPase YscN is part of the type III secretion system, that translocates many virulence-related, bacterial effector proteins directly into the cytosol of host cells
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system delivers bacterial effector proteins into host cells that then modulates host cellular functions
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
?
ATP + H2O
ADP + phosphate
-
pathogens use the type III system as a key virulence mechanism
-
-
-
ATP + H2O
ADP + phosphate
-
the type III secretion mechanism enables Yersinia sp. to inject a number of essential virulence determinants into the cytosol of host target cells. The injected proteins appear to interfere with host cell signal transduction pathway and other cellular processes, allowing Yersinia sp. to obstruct the primary immune response and to establish a systemic infaction
-
-
-
ATP + H2O
ADP + phosphate
-
YscU is an ATPase and a component of the Yersinia type III secretion machine, YscN is regulated by YscL, which binds YscU, an autocatalytically cleaving protease of the complex, YscN and YscU do not bind directly in vivo, interaction analysis, overview
-
-
?
additional information
?
-
-
PilB and PilT are bipolar proteins belonging to the secretion NTPase superfamily, and power pilus extension and retraction, respectively, while the unipolar PilT paralogue PilU supports pilus retraction in an unknown manner. In all three proteins, the third acidic residue in the Asp Box and the second His of the His Box are crucial for function, mutation of these residues causes loss of PilT ATPase activity in vitro
-
-
-
additional information
?
-
-
PilB and PilT are bipolar proteins belonging to the secretion NTPase superfamily, and power pilus extension and retraction, respectively, while the unipolar PilT paralogue PilU supports pilus retraction in an unknown manner. In all three proteins, the third acidic residue in the Asp Box and the second His of the His Box are crucial for function, mutation of these residues causes loss of PilT ATPase activity in vitro
-
-
-
additional information
?
-
enzyme SsaN binds to Salmonella pathogenicity island 2 (SPI-2) specific chaperones, including SsaE, SseA, SscA, and SscB that facilitate translocator/effector secretion, SsaN dissociates a chaperone-effector complex, SsaE and SseB, in an ATP-dependent manner. Effector release is dependent on a conserved arginine residue at position 192 of SsaN, and this is essential for its enzymatic activity
-
-
-
additional information
?
-
FliI is the ATPase energy donor of the flagellar type III export apparatus, interactions of flagellar chaperones with ATPase FliI, overview. FliT and the FliT-FliD complex bind to FliI
-
-
-
additional information
?
-
T3SS ATPases functions as a docking site for chaperone-effector complexes, molecular mechanism by which SsaN captures these complexes to initiate translocation and recognizes the chaperones, overview. Modeling of the interaction between the multicargo chaperone, SrcA, and enzyme SsaN and validation of the model using SrcA mutagenesis to identify the residues on both the chaperone and ATPase that mediate the interaction
-
-
-
additional information
?
-
enzyme SsaN binds to Salmonella pathogenicity island 2 (SPI-2) specific chaperones, including SsaE, SseA, SscA, and SscB that facilitate translocator/effector secretion, SsaN dissociates a chaperone-effector complex, SsaE and SseB, in an ATP-dependent manner. Effector release is dependent on a conserved arginine residue at position 192 of SsaN, and this is essential for its enzymatic activity
-
-
-
additional information
?
-
-
stability of HrcN depends on the conserved HrcL protein, which interacts with HrcN in vitro and in vivo, overexpression of HrcL affects bacterial pathogenicity. HrcN also interacts with the T3S substrate specificity switch protein HpaC and the global T3S chaperone HpaB, which promotes secretion of multiple effector proteins, protein-protein interaction studies, overview
-
-
-
additional information
?
-
-
HrcN dissociates a complex between HpaB and the effector protein XopF1 in an ATP-dependent manner. The effector release depends on a conserved glycine residue in the HrcN phosphate-binding loop, which is crucial for enzymatic activity and protein function during membrane-spanning type III secretion, T3S
-
-
-
additional information
?
-
-
enzyme ATPase HrcN interacts with its regulator HrcL and substrate acceptor site HrcQ
-
-
-
additional information
?
-
-
enzyme ATPase HrcN interacts with its regulator HrcL and substrate acceptor site HrcQ
-
-
-
additional information
?
-
-
YscN does not bind to the fused chaperone SycE with effector YopE, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
HopB1/in + ATP + H2O
HopB1/out + ADP + phosphate
-
intrinsic protein substrate, type II effector of pathogen
-
-
?
HopPtoN/in + ATP + H2O
HopPtoN/out + ADP + phosphate
-
Hrp outer protein effector of pathogen, that is translocated into host cells in enzyme-dependent secretion
-
-
?
HrpJ/in + ATP + H2O
HrpJ/out + ADP + phosphate
-
intrinsic protein substrate, its secretion is required for pathogenicity and translocation of effectors into plant cells
-
-
?
HrpK/in + ATP + H2O
HrpK/out + ADP + phosphate
-
intrinsic protein substrate, C-terminal half of protein is required for translocation
-
-
?
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
-
ATP + H2O
ADP + phosphate
-
the type III secretion system is dependent on ATPase activity, which catalyzes the unfolding of proteins and the secretion of effector proteins through the injectisome. CdsN, Cpn0707, is the T3S ATPase. CdsN interacts with CdsD, CdsL, CdsQ, and CopN, four putative structural components of the T3S system, CdsN also interacts with an unannotated protein, Cpn0706, a putative CdsN chaperone, overview
-
-
?
ATP + H2O
ADP + phosphate
Chlamydia pneumoniae CWL-029 / ATCC VR1310
-
the type III secretion system is dependent on ATPase activity, which catalyzes the unfolding of proteins and the secretion of effector proteins through the injectisome. CdsN, Cpn0707, is the T3S ATPase. CdsN interacts with CdsD, CdsL, CdsQ, and CopN, four putative structural components of the T3S system, CdsN also interacts with an unannotated protein, Cpn0706, a putative CdsN chaperone, overview
-
-
?
ATP + H2O
ADP + phosphate
-
the cloned Erwinia chrysanthemi Hrp type III protein secretion system functions in Escherichia coli to deliver Pseudomonas syringae Avr signals to plant cells and to secrete Avr proteins in culture
-
?
ATP + H2O
ADP + phosphate
-
type II enzyme system: secretion of a large number of enzymes, including cellulases and pectinases
-
?
ATP + H2O
ADP + phosphate
-
in addition the protein binds DNA and interacts with PcfF and PcfG
-
-
ir
ATP + H2O
ADP + phosphate
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
-
ATP + H2O
ADP + phosphate
-
secretion of pectic enzymes and cellulase by the type II secretion system
-
-
-
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
-
ATP + H2O
ADP + phosphate
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
-
ATP + H2O
ADP + phosphate
-
PilB and PilT of the type IV pili, T4P, system in Myxococcus xanthus have ATPase activity acting at distinct steps in the T4P extension/retraction cycle in vivo
-
-
?
ATP + H2O
ADP + phosphate
-
PilB and PilT of the type IV pili, T4P, system in Myxococcus xanthus have ATPase activity acting at distinct steps in the T4P extension/retraction cycle in vivo
-
-
?
ATP + H2O
ADP + phosphate
-
type III secretion system is required for secretion of pectinase and cellulase
-
-
-
ATP + H2O
ADP + phosphate
-
secretion of elastase, exotoxin A, phospholipase C, and other proteins
-
-
-
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
-
ATP + H2O
ADP + phosphate
-
the Hrp type III protein secretion system catalyzes the Hrp pilus assembly
-
-
-
ATP + H2O
ADP + phosphate
-
secretion of the avirulence proteins HrmA and AvrPto from Pseudomonas syringae pathovars
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
FliH regulates the activity of the FliI ATPase and binds to FliI suppressing its oligomerization and ATPase activity. At the level of the export ATPase complex, two activities have been reported for FliJ, i.e. a T3SS chaperone escort activity and a stimulation of the FliI ATPase activity
-
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
FliI, an ATPase, provides the energy for export of the protein subunits, that form the filament and other structures to outside the membrane, via a specialized secretion apparatus, overview. This apparatus is related to the injectisome used by many gram-negative pathogens and symbionts to transfer effector proteins into host cells by type III secretion mechanism. Flagellar secretion in Salmonella enterica requires the proton motive force and does not require ATP hydrolysis by FliI. FliI is non-essential for flagellar assembly and function
-
-
?
ATP + H2O
ADP + phosphate
-
type III protein-secretion system delivers bacterial proteins into host cells that mediate this bacterium“s ability to enter nonpathogenic cells
-
-
-
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
the two type II secretion systems, SPI-1 and SPI-2 appear to play different roles during pathogenesis, with SPI-1 being required for initial penetration of the intestinal mucosa and SPI-2 necessary for subsequent systemic stages of infection
-
-
-
ATP + H2O
ADP + phosphate
-
FliI, the ATPase involved in bacterial flagellar protein export, forms a complex with its regulator FliH in the cytoplasm and hexamerizes upon docking to the export gate composed of integral membrane proteins
-
-
?
ATP + H2O
ADP + phosphate
-
FliI, the ATPase involved in bacterial flagellar protein export, forms a complex with its regulator FliH in the cytoplasm and hexamerizes upon docking to the export gate composed of integral membrane proteins
-
-
?
ATP + H2O
ADP + phosphate
-
type III protein-secretion system delivers bacterial proteins into host cells that mediate this bacterium“s ability to enter nonpathogenic cells
-
-
-
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
pathogens use the type III system as a key virulence mechanism
-
-
-
ATP + H2O
ADP + phosphate
-
invasion of epithelial cells by Shigella flexneri is mediated by a set of translocated bacterial invasins, the Ipa proteins, and its dedicated type III secretion system, Mxi-Spa
-
-
?
ATP + H2O
ADP + phosphate
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
-
ATP + H2O
ADP + phosphate
-
secretion of AvrBs2 to pepper plants
-
-
-
ATP + H2O
ADP + phosphate
-
type II secretion is the primary pathway for the secretion of extracellular degradative enzymes by gram-negative bacteria
-
-
-
ATP + H2O
ADP + phosphate
-
The membrane-spanning type III secretion, T3S, system injects effector proteins into the cytosol of eukaryotic host cells, the T3S apparatus is associated with an ATPase that presumably provides the energy for the secretion process. HrcN is crucial for effector protein translocation and is essential for T3S and bacterial pathogenicity
-
-
?
ATP + H2O
ADP + phosphate
-
XpsE is the key component of the multi-protein complex of the type II secretion system T2SS, comprising 12 protein components, regulation occurs via Clp, a homologue of the cyclic AMP-receptor protein, by directly binding to the xpsE promoter region, overview
-
-
?
ATP + H2O
ADP + phosphate
Yersinia enterolytica
-
pathogenic bacteria use protein secretion system type II and type IV to deliver microbial avirulence proteins and transfer DNA-protein complexes directly into plant cells
-
-
-
ATP + H2O
ADP + phosphate
-
the ATPase YscN is part of the type III secretion system, that translocates many virulence-related, bacterial effector proteins directly into the cytosol of host cells
-
-
?
ATP + H2O
ADP + phosphate
-
secreted proteins, their biochemical activity and interaction with host or other proteins, overview
-
-
-
ATP + H2O
ADP + phosphate
-
pathogens use the type III system as a key virulence mechanism
-
-
-
ATP + H2O
ADP + phosphate
-
the type III secretion mechanism enables Yersinia sp. to inject a number of essential virulence determinants into the cytosol of host target cells. The injected proteins appear to interfere with host cell signal transduction pathway and other cellular processes, allowing Yersinia sp. to obstruct the primary immune response and to establish a systemic infaction
-
-
-
ATP + H2O
ADP + phosphate
-
YscU is an ATPase and a component of the Yersinia type III secretion machine, YscN is regulated by YscL, which binds YscU, an autocatalytically cleaving protease of the complex, YscN and YscU do not bind directly in vivo, interaction analysis, overview
-
-
?
additional information
?
-
-
PilB and PilT are bipolar proteins belonging to the secretion NTPase superfamily, and power pilus extension and retraction, respectively, while the unipolar PilT paralogue PilU supports pilus retraction in an unknown manner. In all three proteins, the third acidic residue in the Asp Box and the second His of the His Box are crucial for function, mutation of these residues causes loss of PilT ATPase activity in vitro
-
-
-
additional information
?
-
-
PilB and PilT are bipolar proteins belonging to the secretion NTPase superfamily, and power pilus extension and retraction, respectively, while the unipolar PilT paralogue PilU supports pilus retraction in an unknown manner. In all three proteins, the third acidic residue in the Asp Box and the second His of the His Box are crucial for function, mutation of these residues causes loss of PilT ATPase activity in vitro
-
-
-
additional information
?
-
A0A0H3NB84
enzyme SsaN binds to Salmonella pathogenicity island 2 (SPI-2) specific chaperones, including SsaE, SseA, SscA, and SscB that facilitate translocator/effector secretion, SsaN dissociates a chaperone-effector complex, SsaE and SseB, in an ATP-dependent manner. Effector release is dependent on a conserved arginine residue at position 192 of SsaN, and this is essential for its enzymatic activity
-
-
-
additional information
?
-
Q8Z5R8
FliI is the ATPase energy donor of the flagellar type III export apparatus, interactions of flagellar chaperones with ATPase FliI, overview. FliT and the FliT-FliD complex bind to FliI
-
-
-
additional information
?
-
P74857
T3SS ATPases functions as a docking site for chaperone-effector complexes, molecular mechanism by which SsaN captures these complexes to initiate translocation and recognizes the chaperones, overview. Modeling of the interaction between the multicargo chaperone, SrcA, and enzyme SsaN and validation of the model using SrcA mutagenesis to identify the residues on both the chaperone and ATPase that mediate the interaction
-
-
-
additional information
?
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A0A0H3NB84
enzyme SsaN binds to Salmonella pathogenicity island 2 (SPI-2) specific chaperones, including SsaE, SseA, SscA, and SscB that facilitate translocator/effector secretion, SsaN dissociates a chaperone-effector complex, SsaE and SseB, in an ATP-dependent manner. Effector release is dependent on a conserved arginine residue at position 192 of SsaN, and this is essential for its enzymatic activity
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-
-
additional information
?
-
-
stability of HrcN depends on the conserved HrcL protein, which interacts with HrcN in vitro and in vivo, overexpression of HrcL affects bacterial pathogenicity. HrcN also interacts with the T3S substrate specificity switch protein HpaC and the global T3S chaperone HpaB, which promotes secretion of multiple effector proteins, protein-protein interaction studies, overview
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-
-
additional information
?
-
-
enzyme ATPase HrcN interacts with its regulator HrcL and substrate acceptor site HrcQ
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-
-
additional information
?
-
-
enzyme ATPase HrcN interacts with its regulator HrcL and substrate acceptor site HrcQ
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mn2+
-
Mg2+ can be substituted by Mn2+, although the reaction rate is reduced by 50%
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FliH
Because FliH suppresses ATP hydrolysis by FliI, FliH coordinates ATP hydrolysis by FliI with protein export. The first 20 residues of FliI (FliIEN) not only regulate FliI ring formation but also are involved in the interaction with FliH
-
hypothetical protein YE3555 termed YsaL
identification and evaluation of a negative regulator of YsaN, a hypothetical protein YE3555, termed YsaL. Purified YsaL is dimeric in solution and strongly associates with YsaN to form a stable heterotrimeric YsaL-YsaN complex with a stoichiometry of 2:1. The N terminal 6-20 residues of YsaN are invariably required for stable YsaL-YsaN complex formation. YsaL inhibits the ATPase activity of YsaN with a maximum inhibition at the molar ratio 2:1 (YsaL: YsaN). Protein YE3555 has a close evolutionary relationship with the T3S ATPase regulators. Identification of critical residues of YsaN for stable YsaL-YsaN complex formation, overview
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N'-[(E)-(2,4-dihydroxyphenyl)methylidene]-4-nitrobenzohydrazide
A0A0C6EWK5
a type III secretion system inhibitor
N'-[(E)-(3,5-dibromo-2-hydroxyphenyl)methylidene]pyridine-3-carbohydrazide
A0A0C6EWK5
a type III secretion system inhibitor
YscN
-
intrinsic regulatory protein, noncompetitive inhibition by allosteric binding
-
additional information
-
fusion of YopR secretion substrate to dihydrofolate reductase results in binding to enzyme and blocking of the type III secretion pathway
-
additional information
-
identification of small molecule inhibitors with IC50 values below 0.02 mM in an in vitro ATPase assay
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FliH
-
the stimulation of the FliI ATPase activity by FliJ occurs either via a transient FliJ-FliI interaction or via interactions of FliJ with other flagellar components, e.g. the FliH protein, the flagellar counterpart of HrpE, with a predicted coiled-coil structure. FliH is a known regulator of FliI activity that binds to FliI and suppresses its oligomerization and ATPase activity
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cardiolipin
stimulates activity of full-length GspEEpsE when in complex with the cytoplasmic domain of GspLEpsL
additional information
hexamerization enhances the ATPase activity of recombinant DN1GspEEpsE-linker-Hcp1 variants compared to monomeric DN1GspEEpsE by more than 20fold
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additional information
-
hexamerization enhances the ATPase activity of recombinant DN1GspEEpsE-linker-Hcp1 variants compared to monomeric DN1GspEEpsE by more than 20fold
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additional information
the cytoplasmic ATPase activity, when copurified with the cytoplasmic domain of an interactive ATPase partner, is stimulated by an acidic phospholipid
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.22
MgATP
-
pH 7.5, 37°C, ATPase activity of N-terminal cytoplasmic domain
0.81
ATP
purified recombinant SsaN-Myc-His6 enzyme, pH 8.0, 37°C
additional information
additional information
-
enzyme shows positive cooperativity and non-Michaelis-Menten kinetics
-
additional information
additional information
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the enzyme shows positive cooperativity
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00525
ATP
-
XpsE, N-domain removed + MBP-tagged XpsL, residues 1-215
0.00558
ATP
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XpsE mutant R286A, N-domain removed + MBP-tagged XpsL, residues 1-215
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.55
-
wild-type full-length CdsN and C-terminal truncation mutant of CdsN, ATPase activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
additional information
-
secretion of the avirulence proteins HrmA and AvrPto from Pseudomonas syringae pathovars is highest at pH 6.0 of the culture medium
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
28
37
additional information
-
secretion of the avirulence proteins HrmA and AvrPto from Pseudomonas syringae pathovars is highest at growth temperature 18-22°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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a number of the Out apparatus components possess domains in the cytoplasm and/or the periplasm with potential for protein-protein interactions which facilitate the secretion of periplasmic enzyme intermediates across the outer membrane to the external milieu. OutC is a cytoplasmic membrane protein with a single transmembrane domain and a large hydrophilic periplasmic domain, OutF is a cytoplasmic membrane protein with three transmembrane domains, a small periplasmic loop, a large cytoplasmic loop and an N-terminal cytoplasmic domain
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additional information
assembly of the ATPase complex to the export gate, model, overview
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a peripheral membrane protein located at the cytoplasmic side
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a number of the Out apparatus components possess domains in the cytoplasm and/or the periplasm with potential for protein-protein interactions which facilitate the secretion of periplasmic enzyme intermediates across the outer membrane to the external milieu. OutC is a cytoplasmic membrane protein with a single transmembrane domain and a large hydrophilic periplasmic domain, OutF is a cytoplasmic membrane protein with three transmembrane domains, a small periplasmic loop, a large cytoplasmic loop and an N-terminal cytoplasmic domain
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the enzyme binds to the membrane-located type III secretion system complex
the T2S ATPase cycles between a cytoplasmic and a membrane-associated state in a secretion-related manner
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the enzyme binds to the membrane-located type III secretion system complex
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-
EscC, outer membrane, EscV, inner membrane fraction, EscN, inner membrane fraction
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a peripheral membrane protein located at the cytoplasmic side
peripheral membrane protein, associates with inner membrane
SsaN and its complex colocalize to the membrane fraction under type III secretion system T3SS-2 inducing conditions, SsaN, SsaK, and SsaQ co-localize to bacterial membranes after T3SS activation
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SsaN and its complex colocalize to the membrane fraction under type III secretion system T3SS-2 inducing conditions, SsaN, SsaK, and SsaQ co-localize to bacterial membranes after T3SS activation
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stability of HrcN in depends on the conserved HrcL protein, which interacts with HrcN in vitro and in vivo, both HrcN and HrcL bind to the inner membrane protein HrcU and specifically localize to the bacterial membranes under T3S-permissive conditions, overview
the T2S ATPase cycles between a cytoplasmic and a membrane-associated state in a secretion-related manner, T2S ATPase may directly associate with the membrane
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the both SspB and SspC, components of the translocation apparatus, are inserted into the host epithelial cell plasma membrane 15 min after Salmonella typhimurium infection, this is required for subsequent translocation of bacterial effector molecules
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the lipidated protein MxiM, required in type III secretion, is anchored to the inner leaflet of the outer membrane
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association of the cytoplasmic membrane protein XpsN with the outer membrane protein XpsD
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
39000
-
1 * 62000, recombinant His-tagged PilB, SDS-PAGE, x * 63800, about, His6-tagged PilB, sequence calculation, 1 * 39000, recombinant His-tagged PilT, SDS-PAGE, 1 * 41000, about, His6-tagged PilT, sequence calculation
41000
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1 * 62000, recombinant His-tagged PilB, SDS-PAGE, x * 63800, about, His6-tagged PilB, sequence calculation, 1 * 39000, recombinant His-tagged PilT, SDS-PAGE, 1 * 41000, about, His6-tagged PilT, sequence calculation
48000
48100
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x * 48100, about, sequence calculation, SDS-PAGE, CdsN forms oligomers and high-molecular-weight multimers, possibly dodecamers
49500
12 * 49500, recombinant His-tagged enzyme, SDS-PAGE. The enzyme exists in solution as higher order oligomer. The ATPase activity of oligomeric YsaN is several fold higher than the activity of the monomeric form
60000
62000
63800
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1 * 62000, recombinant His-tagged PilB, SDS-PAGE, x * 63800, about, His6-tagged PilB, sequence calculation, 1 * 39000, recombinant His-tagged PilT, SDS-PAGE, 1 * 41000, about, His6-tagged PilT, sequence calculation
603000
recombinant His-tagged enzyme dodecamer, gel filtration
additional information
60000
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His6-PcfCdeltaN103, determined by size exclusion chromatography
62000
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1 * 62000, recombinant His-tagged PilB, SDS-PAGE, x * 63800, about, His6-tagged PilB, sequence calculation, 1 * 39000, recombinant His-tagged PilT, SDS-PAGE, 1 * 41000, about, His6-tagged PilT, sequence calculation
additional information
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length of proteins in amino acids
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dodecamer
hexamer
homohexamer
monomer
oligomer
trimer
3 * 83000, GspE-cyto-GspL complex, crystal structure analysis
additional information
dodecamer
12 * 48000, SDS-PAGE, predominant form at membrane, activity increases 700fold over monomeric form
dodecamer
12 * 49500, recombinant His-tagged enzyme, SDS-PAGE. The enzyme exists in solution as higher order oligomer. The ATPase activity of oligomeric YsaN is several fold higher than the activity of the monomeric form
hexamer
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full-length EscN forms a stable hexamer in solution with stimulated ATPase activity
hexamer
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nucleotide binding locks enzyme hexamer into a symmetric and compact structure, in absence of nucleotide, the N-terminal domain exhibits a collection of rigid-body conformations, crystallization data and analytical ultracentrifugation
hexamer
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FliI forms a complex with its regulator FliH in the cytoplasm and hexamerizes upon docking to the export gate composed of integral membrane proteins
hexamer
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FliI forms a complex with its regulator FliH in the cytoplasm and hexamerizes upon docking to the export gate composed of integral membrane proteins
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homohexamer
fully active enzyme form, FliI forms hetero-trimers along with the FliH dimer
homohexamer
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secretion NTPases of the type II secretion and type IV pili systems, including PilB, PilT and PilU, function as toroidal homohexamers and, in addition toWalker A and Walker B motifs, contain unique Asp Box and His Box motifs
homohexamer
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secretion NTPases of the type II secretion and type IV pili systems, including PilB, PilT and PilU, function as toroidal homohexamers and, in addition toWalker A and Walker B motifs, contain unique Asp Box and His Box motifs
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homohexamer
a two-helix-finger motif and a conserved loop located at the entrance of and within the predicted pore formed by the hexameric ATPase, structure modeling
homohexamer
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a two-helix-finger motif and a conserved loop located at the entrance of and within the predicted pore formed by the hexameric ATPase, structure modeling
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monomer
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1 * 62000, recombinant His-tagged PilB, SDS-PAGE, x * 63800, about, His6-tagged PilB, sequence calculation, 1 * 39000, recombinant His-tagged PilT, SDS-PAGE, 1 * 41000, about, His6-tagged PilT, sequence calculation
monomer
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1 * 62000, recombinant His-tagged PilB, SDS-PAGE, x * 63800, about, His6-tagged PilB, sequence calculation, 1 * 39000, recombinant His-tagged PilT, SDS-PAGE, 1 * 41000, about, His6-tagged PilT, sequence calculation
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oligomer
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x * 48100, about, sequence calculation, SDS-PAGE, CdsN forms oligomers and high-molecular-weight multimers, possibly dodecamers
oligomer
Chlamydia pneumoniae CWL-029 / ATCC VR1310
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x * 48100, about, sequence calculation, SDS-PAGE, CdsN forms oligomers and high-molecular-weight multimers, possibly dodecamers
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oligomer
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different oligomeric forms are identified by blue native electrophoresis, including a hexamer and a dodecamer
additional information
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enzyme associates with intrinsic protein exeB to forms large complexes
additional information
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fliI encodes a 50000 Da polypeptide ATPase, fliJ encodes a 16000 Da hydrophobic protein of unknown function
additional information
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the outer-membrane lipoprotein OutS interacts directly with the C-terminal end of the secretin OutD
additional information
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the Out proteins form a membrane-associated multiprotein complex, OutE is the putative ATP binding component and OutL is an inner membrane protein. OutE and OutL interact directly. OutE induces a conformational change in OutL, in both its cytoplasmic and periplasmic domains. The secretion process requires a conformational change in OutE which depends on both the interaction with OutL and on the presence of an intact Walker A motif in OutE
additional information
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the secretory pathway comprises a number of inner membrane proteins, SecD to SecF, SecY, a cytoplasmic membrane-associated ATPase, SecA, that provides the energy for export, a chaperone, SecB, that binds to presecretory target proteins, and the periplasmic signal peptidase
additional information
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effector Tir is not required for chaperone and enzyme interactions, enzyme binds effector specifically without its chaperone
additional information
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PilB and PilT proteins do not form oligomers under all conditions tested, overview
additional information
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PilB and PilT proteins do not form oligomers under all conditions tested, overview
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additional information
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Out C, OutD, OutE and OutF are proteins of the Put apparatus, OutC is a cytoplasmic membrane protein with a single transmembrane domain and a large hydrophilic periplasmic domain, OutF is a cytoplasmic membrane protein with three transmembrane domains, a small periplasmic loop, a large cytoplasmic loop and an N-terminal cytoplasmic domain
additional information
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the general secretion pathway requires the participation of 12 proteins, of which XcpT, XcpU, XcpV, XcpW are homologues of PilA, the major subunit of type IV pili. PilA itself is necessary for optimal secretion of proteins demonstrating that the pathway of type IV pilus assembly and the operation of the apparatus of the general secretion pathway are overlapping processes
additional information
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several components of the type III secretion system are organized in a supramolecular structure termed needle complex. This structure is made of discrete structures including a base that spans both membranes and a needle-like projection that extends outwards from the bacterial surface. The type III secretion export apparatus is required for the assembly of the needle substructure but is dispensable for the assembly of the base. The length of the needle segment is determined by the type III secretion associated protein InvJ. InvG, PrgH, and PrgK constitute the base. PrgI is the main component of the needle of the type III secretion complex. The needle component may establish the specificity of type III secretion system in delivering proteins into either plant or animal cells
additional information
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model of domain construction and complex of subunits
additional information
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structure analysis and comparison using crystal structure PDB code DPY
additional information
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structure analysis and comparison using crystal structure PDB code DPY
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additional information
-
several components of the type III secretion system are organized in a supramolecular structure termed needle complex. This structure is made of discrete structures including a base that spans both membranes and a needle-like projection that extends outwards from the bacterial surface. The type III secretion export apparatus is required for the assembly of the needle substructure but is dispensable for the assembly of the base. The length of the needle segment is determined by the type III secretion associated protein InvJ. InvG, PrgH, and PrgK constitute the base. PrgI is the main component of the needle of the type III secretion complex. The needle component may establish the specificity of type III secretion system in delivering proteins into either plant or animal cells
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additional information
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the lipidated protein MxiM is required in type III secretion
additional information
recombinant enzyme GspE-Hcp1 fusion proteins, i.e. DELTAN1GspEEpsE-KLASGHcp1, DELTAN1GspEEpsE-GSGSGS-Hcp1, DELTAN1GspEEpsE-KLASGAGHcp1, and DELTAN1GspEEpsE-KLASGAGH-Hcp1, show homogeneous hexamer formation, structure analysis, detailed overview. The hexamerization enhances the ATPase activity of these four DN1GspEEpsE-linker-Hcp1 variants compared to monomeric DN1GspEEpsE by more than 20fold. The metal binding domains are located on the periphery of both DN1GspEEpsE hexamers
additional information
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recombinant enzyme GspE-Hcp1 fusion proteins, i.e. DELTAN1GspEEpsE-KLASGHcp1, DELTAN1GspEEpsE-GSGSGS-Hcp1, DELTAN1GspEEpsE-KLASGAGHcp1, and DELTAN1GspEEpsE-KLASGAGH-Hcp1, show homogeneous hexamer formation, structure analysis, detailed overview. The hexamerization enhances the ATPase activity of these four DN1GspEEpsE-linker-Hcp1 variants compared to monomeric DN1GspEEpsE by more than 20fold. The metal binding domains are located on the periphery of both DN1GspEEpsE hexamers
additional information
GspE is a protein of about 500 residues folding into three major domains, the N-terminal domains N1E and N2E, and the C-terminal domain CTE. The N2E and CTE domains of a single GspE subunit adopt a mutual orientation
additional information
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GspE is a protein of about 500 residues folding into three major domains, the N-terminal domains N1E and N2E, and the C-terminal domain CTE. The N2E and CTE domains of a single GspE subunit adopt a mutual orientation
additional information
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analysis of protein-protein interactions of type III secretion system, ATPase HrcN has a hexameric ring structure
additional information
-
association of the cytoplasmic membrane protein XpsN, MW 36000 Da determined by SDS-PAGE, with the outer membrane protein XpsD in the type II protein secretion apparatus
additional information
-
XpsE possesses a nucleotide-binding Walker A motif
additional information
-
upon addition of ATP, purified enzyme forms aggregates, probably hexamers
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
-
the lipidated protein MxiM, required in type III secretion, is anchored to the inner leaflet of the outer membrane
proteolytic modification
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EscC, 56000 Da preprotein is cleaved to 54000 mature protein, EscV, 75000 Da preprotein with sec-dependent signal sequence, 72000 mature protein, EscN, 49000 Da cytoplasmic protein with no signal sequence
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of selenomethionine-substituted afGspE are grown in the presence of 10 mM AMP-PNP and 10 mM Mg2+, a resolution of 2.95 A is attained
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the crystal structure of the catalytic domain of the prototypical T3SS ATPase EscN of Escherichia coli is presented at a resolution of 1.8 A
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cryo-electron microscopy, enzyme dodecamer comprises two hexameric rings that are stacked face-to-face by the association of their C-terminal regions
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purified recombinant wild-type enzyme, hanging drop vapor diffusion method, mixing of 0.002 ml of 1.7 mg/ml protein in 20 mM Tris, pH 7.5, 0.1 M potassium chloride, and 0.01 M tris(2-carboxyethyl)phosphine with 0.001 ml of crystallization solution containing 0.5 M ammonium sulfate, 0.1 M sodium citrate tribasic dihydrate, pH 5.6, and 10% v/v Jeffamine M-600, and 200 nl of 0.1 M L-proline, the drops are initially dehydrated against 0.5 ml of 1.5 M ammonium sulfate, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement and modeling
major cytoplasmic domain of EpsL protein that is part of the ATPase complex
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periplasmic domain of EpsM protein, fold is a circular permutation of the ferredoxin fold
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recombinant enzyme GspE-Hcp1 fusion protein hexamers, sitting drop vapour diffusion method, mixing of 0.001 ml protein solution containing 20 mM Tris-HCl, pH 8.0, 500 mM NaCl, 5% v/v glycerol, 1 mM TCEP/HCl, 5 mM AMPPNP, and 5 mM MgCl2 with different precipitant solutions, containing for DN1GspEEpsE-GSGSGS-Hcp1 7% PEG 6000 and 0.1 M bicine, pH 9.0, for DN1GspEEpsE-KLASGAGH-Hcp1 16% PEG 300, 0.2 M ammonium sulfate, 0.1 M Bis Tris, pH 6.1, 5 mM ADP, 5 mM MgCl2, 5 mM AlCl3, and 15 mM NaF, for DELTAN1GspEEpsE-KLASGAG-Hcp1 7% PEG 3350, 0.12 M ammonium citrate pH 7.0, 5 mM ADP, and 5 mM MgCl2, and for DELTAN1GspEEpsE-KLASG-Hcp1 12.5% PEG 20000, 0.1 M bicine pH 9.0, and 2% v/v 1,4-dioxane, at 4°C, X-ray diffraction structure determination and analysis at 4.09-7.6 A resolution
purified recombinant enzyme GspE in complex with cyto-GspL, sitting drop vapor diffusion method, by mixing of 0.001 ml of protein in 20 mM HEPES, pH7.5, 200 mM NaCl buffer with 0.001 ml of reservoir solution containing 0.2 M Na malonate pH 7.0, 18% PEG 3350, at 21°C, X-ray diffraction structure determination and analysis at 2.83 A resolution, molecular replacement using the structures of Vibrio cholerae DELTAN1EGspE (PDB ID 1P9R) and the Vibrio cholerae N1E-cyto-GspL complex (PDB ID 2BH1) as search models
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stability of HrcN depends on the conserved HrcL protein, which interacts with HrcN in vitro and in vivo
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography, using Talon, Co2+, resin and glutathione-Sepharose beads, and by gel filtration
-
EpsE is copurified with the cytoplasmic domain of EpsL to test whether the ATPase activity of EpsE can be modulated by EpsL, complexes are purified using metal affinity chromatography and gel filtration, monomeric EpsE is obtained following thrombin cleavage of a GST-EpsE fusion protein
-
His-tagged EscN is purified from the soluble fraction using nickel-chelating Sepharose, the tag is cleaved with thrombin, cleaved product is purified by Mono-Q anion exchange
-
partially by subcellular fractionation of wild-type strain DK1622 expressing GFP-tagged wild-type PilB and PilT, recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant FLAG-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by affinity chromatography
recombinant GST-tagged full-length CdsN and CdsN C-terminal truncation mutant from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography
-
recombinant GST-tagged YscP by glutathione affinity chromatography, YscP-GST co-purifies with YscN, YscL, YscQ, and YscO
-
recombinant His10-FLAG3-tagged InvC/FLAG3-tagged OrgB complexes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant SsaN-Myc-His6, EscN-Myc-His6, and SsaNR192G-Myc-His6 wefrom Escherichia coli by nickel affinity chromatography
recombinant Strep-tagged wild-type and mutant enzymes by streptavidin affinity chromatography
-
soluble part of recombinant N-terminally His-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration, recombinant His-tagged truncation mutant enzymes from Escherichia coli strain BL21(DE3) are unfolded, dialysed and refolded and purified by nickel affinity chromatography and gel filtration, recombinant untagged wild-type enzyme
XpsE-Strep and its variants are purified from the Strep-Tactin Sepharose column, the XpsE with His6-tag is purified by eluting from nickel nitrilotriacetate resin
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Yersinia enterocolitica LJ4036, a strain in which the wild-type copy of yscP is deleted from the virulence plasmid
-
expression in Escherichia coli
expression of C-terminally c-Myc-tagged ATPase HrcN under control of the lac promoter into Xanthomonas campestris strains 85-10DhrcQ and 85*DhrcQ, co-expression with GST-HrcQ and C-terminally c-Myc-tagged HrcL in Escherichia coli
-
expression of N-terminally His-tagged wild-type and deletion mutant Flil enzymes, and expression of the deletion mutants in Salmonella typhimurium strain SJW1103
-
expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain JM109, expression of GFP-tagged wild-type PilB and PilT in strain DK1622
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expresssion of GST-tagged full-length CdsN and a C-terminal truncation mutant of CdsN in Escherichia coli strain BL21(DE3)
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gene hrcN, cloned from strain 85-10, co-expression with c-Myc-tagged hrcL in Escherichia coli strain BL21(DE3), expression of Strep-tagged HrcN and Strep-tagged HrcN mutant G175C
-
gene invC, recombinant expression of His10-FLAG3-tagged InvC/FLAG3-tagged OrgB complexes in Escherichia coli strain BL21(DE3)
gene ssaN, recombinant expression of wild-type and mutant enzymes tagged with hemagglutinin, c-Myc, a FLAG- or a His6-tag, in Escherichia coli and Salmonella enterica, co-expression with SsaK-2HA and SsaQ-2HA fusion proteins
gene xpsE, recombinant expression of C-terminally ECFP-tagged enzyme in the xpsE-null strain XC1723 complementing the strain and restoring the secretion activity
gene xpsE, xpsE gene regulation and promoter activity analysis, overview
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gene ysaN, recombinant expression of N-terminally His-tagged wild-type and of His-tagged truncation mutant enzymes in Escherichia coli strain BL21(DE3), expression of untagged wild-type enzyme
gene yscP, expression of GST-fusion YscP in wild-type strain W22703 and strain EC2 DELTA(yscM1 yscM2)
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genes pilB, pilT and pilU from strain PAK, expression of wild-type and mutant enzymes in Escherichia coli strain Bl21(DE3). Expression of YFP-PilT, YFP-PilB, and YFP-PilU fusion enzymes, which retain their characteristic pattern of polar localization, with the exception of the Walker A mutant of YFP-PilT
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into the pET19b vector for expression in Escherichia coli BL21DE3 pLysS cells
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into the pET28a expression vector for expression in Escherichia coli BL21DE3 cells
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nine pcfF expression plasmids are constructed, different in the combination of the promotor, Pnis, P23, Ptac, PT7, the affinity tag, His6, GST, and the cloned PcfC fragment, complete cDNA, deltaN103 or mutant K156T
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plasmids pEpsE/EpsL(1-253)His6 and pEpsE/EpsL(1-242)His6 using pET21d+ are constructed, for expression of monomeric EpsE the vector GST-EpsE is constructed
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recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
recombinant expression of FLAG-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant expression of the enzyme GspE as fusion proteins with Pseudomonas aeruginosa Hcp1, i.e. DELTAN1GspEEpsE-KLASGHcp1, DELTAN1GspEEpsE-GSGSGS-Hcp1, DELTAN1GspEEpsE-KLASGAGHcp1, and DELTAN1GspEEpsE-KLASGAGH-Hcp1 showing homogeneous hexamer formation, several variants of DN1GspEEpsE-Hcp1 fusions with different linker sequences are constructed
the cloned Erwinia chrysanthemi Hrp type III protein secretion system functions in Escherichia coli to deliver Pseudomonas syringae Avr signals to plant cells and to secrete Avr proteins in culture
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using a pET29a based plasmid and pET15b for overexpressing of the protein in Escherichia coli BL21DE3 pLysS cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R18A
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dramatic decrease in hexameric particles, increase ATPase activity
E205A
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a Walker B box substitution in PilT, leads to strong reduction of ATPase activity due to direct interference with ATP hydrolysis
E391A
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a Walker B box substitution in PilB, leads to strong reduction of ATPase activity due to direct interference with ATP hydrolysis
K137A
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a Walker A box substitution in PilT, leads to abolishment of ATPase activity due to indirect interference withe ATP binding
K327A
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a Walker A box substitution in PilB, leads to strong reduction of ATPase activity due to indirect interference withe ATP binding
E205A
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a Walker B box substitution in PilT, leads to strong reduction of ATPase activity due to direct interference with ATP hydrolysis
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E391A
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a Walker B box substitution in PilB, leads to strong reduction of ATPase activity due to direct interference with ATP hydrolysis
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K137A
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a Walker A box substitution in PilT, leads to abolishment of ATPase activity due to indirect interference withe ATP binding
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K327A
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a Walker A box substitution in PilB, leads to strong reduction of ATPase activity due to indirect interference withe ATP binding
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E204
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mutation in the Walker B motif of PilT, and in PilU, inactive PilT mutant
G135S
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mutation in the Asp Box of PilT, and in PilU, inactive PilT mutant
E383A
site-directed mutagenesis, the mutant shows almost unaltered protein secretion activity compared to the wild-type
E384A
site-directed mutagenesis, the mutant shows reduced protein secretion activity compared to the wild-type
E384A/Y385A
site-directed mutagenesis, the mutant shows reduced protein secretion activity compared to the wild-type
E384A/Y385A/G388A
site-directed mutagenesis, the mutant shows markedly reduced protein secretion activity and reduced ATPase activity compared to the wild-type
G164C
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loss-of-function mutant, unable to hydrolyze ATP, decrease in ability to interact with themselves and wild-type enzyme molecules
G388A
site-directed mutagenesis, the mutant shows slightly reduced protein secretion activity compared to the wild-type
K165E
site-directed mutagenesis, InvC ATPase inactive enzyme mutant
L376P
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loss-of-function mutant, defective in type II secretion and infection of cultured cells, wild-type ATP-ase activity
R191H
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loss-of-function mutant, unable to hydrolyze ATP, decrease in ability to interact with themselves and wild-type enzyme molecules
R192G
site-directed mutagenesis of the conserved arginine residue at position 192 of SsaN located in the dicyclohexylcarbodiimide-binding site in the catalytic domain, inactive mutant showing no ATPase and translocation activity. Introducing a plasmid that expresses SsaNR192G into the DELTAssaN mutant fails to complement SseJ secretion. Mutant SsaNR192G-Myc-His6 binds to chaperone SsaE
V28M
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loss-of-function mutant, defective in type II secretion and infection of cultured cells, wild-type ATP-ase activity
V51E
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loss-of-function mutant, defective in type II secretion and infection of cultured cells, wild-type ATP-ase activity
Y385A
site-directed mutagenesis, the Salmonelly typhimurium mutant strain expressing InvCY385A shows a marked defect in its ability to secrete the effector proteins SptP and SopB, while expression of the substrate proteins is unaffected by introduction of mutations in InvC, the mutant shows reduced ATPase activity compared to the wild-type
Y385W
site-directed mutagenesis, the mutant shows reduced ATPase activity compared to the wild-type
E383A
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site-directed mutagenesis, the mutant shows almost unaltered protein secretion activity compared to the wild-type
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E384A
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site-directed mutagenesis, the mutant shows reduced protein secretion activity compared to the wild-type
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R192G
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site-directed mutagenesis of the conserved arginine residue at position 192 of SsaN located in the dicyclohexylcarbodiimide-binding site in the catalytic domain, inactive mutant showing no ATPase and translocation activity. Introducing a plasmid that expresses SsaNR192G into the DELTAssaN mutant fails to complement SseJ secretion. Mutant SsaNR192G-Myc-His6 binds to chaperone SsaE
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Y385A
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site-directed mutagenesis, the Salmonelly typhimurium mutant strain expressing InvCY385A shows a marked defect in its ability to secrete the effector proteins SptP and SopB, while expression of the substrate proteins is unaffected by introduction of mutations in InvC, the mutant shows reduced ATPase activity compared to the wild-type
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Y385W
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site-directed mutagenesis, the mutant shows reduced ATPase activity compared to the wild-type
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R286A
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XpsE mutant hydrolysis ATP at a rate five times that of the wild-type XpsE, but is non-functional in protein secretion via T2SS
K175E
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mutation in one of hte Walker boxes, enzymatically inactive
additional information
additional information
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expression of N-terminal cytoplasmic domain, domain shows ATPase activity
additional information
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generation of a bsaS deletion mutant, the bsaS deletion mutant is highly attenuated for virulence in BALB/c mice
additional information
generation of a bsaS deletion mutant, the bsaS deletion mutant is highly attenuated for virulence in BALB/c mice
additional information
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generation of a bsaS deletion mutant, the bsaS deletion mutant is highly attenuated for virulence in BALB/c mice
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additional information
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the GST-tagged C-terminal truncation mutant of CdsN possesses ATPase activity
additional information
Chlamydia pneumoniae CWL-029 / ATCC VR1310
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the GST-tagged C-terminal truncation mutant of CdsN possesses ATPase activity
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additional information
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escV nonpolar deletion mutant, accumulation of EscC in periplasm. escN nonpolar deletion mutant, accumulation of EscC in periplasm
additional information
gene disruption mutant, shows reduced secretion of pilD-dependent enzymatic activities, mutants are greatly impaired for growth within Hartmannella vermiformis. Upon infection of U937 macrophages, mutant strains exhibit a 10fold reduction in intracellular multiplication and a diminished cytopathic effect
additional information
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construction of diverse Walker A and Walker B boxe mutants, PilB as well as PilT ATPase activity is abolished in vitro by replacement of conserved residues in the Walker A and Walker B boxes that are involved in ATP binding and hydrolysis, respectively, cell phenotypes, overview
additional information
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construction of diverse Walker A and Walker B boxe mutants, PilB as well as PilT ATPase activity is abolished in vitro by replacement of conserved residues in the Walker A and Walker B boxes that are involved in ATP binding and hydrolysis, respectively, cell phenotypes, overview
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additional information
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a spa47 mutant is constructed by inserting a kanamycin-resistance gene into the spa47 gene, spa47 encodes a putative ATPase, the mutant HI4320spa47omegakan displays no growth defect
additional information
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a constructed YFP-PilB construct does not complement a pilB mutant, mutation of conserved Walker A or Walker B residues in any of PilB, PilT and PilU ATPases abrogates twitching motility, and for the Walker A mutant of PilT causes loss of polar localization, overview
additional information
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weak swarming motility and rare flagella are observed in a mutant deleted for FliI and for the nonflagellar type III secretion ATPases InvJ and SsaN
additional information
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deletion mutants of regulatory protein FliH, deletion of last five residues causes 5fold activation of ATPase activity, FliH N-terminus stabilizes complex with ATPase subunit, residues between 99 and 235 required for interaction with ATPase
additional information
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generation of in-frame 10-residue deletion mutations within the 100 residues of the N-terminal domain. The oligomerization and FliH-binding ability are retained and the ATPase activity is maintained in most of the deletion variants, except for DELTA6 mutant and partially for DELTA1 mutant, DELTA4 mutant shows inhibited motility compared to the wild-type enzyme, mutant DELTA2 and DELTA4, as well as DELTA35-38 show 1.3, 5.7, and 2fold increased ATPase activity, overview
additional information
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generation of in-frame 10-residue deletion mutations within the 100 residues of the N-terminal domain. The oligomerization and FliH-binding ability are retained and the ATPase activity is maintained in most of the deletion variants, except for DELTA6 mutant and partially for DELTA1 mutant, DELTA4 mutant shows inhibited motility compared to the wild-type enzyme, mutant DELTA2 and DELTA4, as well as DELTA35-38 show 1.3, 5.7, and 2fold increased ATPase activity, overview
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additional information
four hexamers of Vibrio cholerae GspEEpsE are obtained when fused to Hcp1 as an assistant hexamer, shown with native mass spectrometry. The enzymatic activity of the GspEEpsE-Hcp1 fusions is about 20 times higher than that of a GspEEpsE monomer. Crystal structures of GspEEpsE-Hcp1 fusions with different linker lengths reveal regular and elongated hexamers of GspEEpsE with major differences in domain orientation within subunits, and in subunit assembly
additional information
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four hexamers of Vibrio cholerae GspEEpsE are obtained when fused to Hcp1 as an assistant hexamer, shown with native mass spectrometry. The enzymatic activity of the GspEEpsE-Hcp1 fusions is about 20 times higher than that of a GspEEpsE monomer. Crystal structures of GspEEpsE-Hcp1 fusions with different linker lengths reveal regular and elongated hexamers of GspEEpsE with major differences in domain orientation within subunits, and in subunit assembly
additional information
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overexpression of the clp gene in Xcc wild-type strain 8004 enhances the production of XpsE as well as endoglucanase and extracellular polysaccharide. Deactivation of the clp gene by Tn5 transposon insertion at the coding sequence of the clp gene, resulting in mutant XC472, reduces XpsE expression levels, overview
additional information
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GST fusions of the cytoplasmic T3S ATPase HrcN and its predicted regulator HrcL are immobilized on glutathione sepharose and incubated with a bacterial lysate containing HrcQ-c-Myc, binding and interaction analysis, overview
additional information
fluorescent-tagged ATPase expressed in secretion-proficient cells is mainly diffused in cytoplasm. Focal spots at the cell periphery are detectable only in a few cells. The discrete foci are augmented in abundance and intensity when the secretion channel is depleted and the exoprotein overproduced, overview. The foci abundance is inversely related to secretion efficiency of the secretion channel. Restored function of the secretion channel paralleles reduced ATPase foci abundance
additional information
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GST fusions of the cytoplasmic T3S ATPase HrcN and its predicted regulator HrcL are immobilized on glutathione sepharose and incubated with a bacterial lysate containing HrcQ-c-Myc, binding and interaction analysis, overview
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additional information
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fusion of YscP with glutathione S-transferase leads to blockage of type III secretion and formation of type III secretion needles requiring the YscP secretion signal sequence, mutational analysis of sequences required for the blockage, overview
additional information
generation of several truncation mutants of YsaN for identification of critical residues of YsaN for stable YsaL-YsaN complex formation, overview. Crosslinking of purified His-tagged enzyme YsaN and His-tagged regulator YsaL, pH 8.0, 25°C, using 0.5 mM ethylene glycol bis(sulfosuccinimidylsuccinate) and 1.5% glutaraldehyde, respectively
additional information
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generation of several truncation mutants of YsaN for identification of critical residues of YsaN for stable YsaL-YsaN complex formation, overview. Crosslinking of purified His-tagged enzyme YsaN and His-tagged regulator YsaL, pH 8.0, 25°C, using 0.5 mM ethylene glycol bis(sulfosuccinimidylsuccinate) and 1.5% glutaraldehyde, respectively
additional information
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three different strains expressing simultaneously a short and a long version of YscP are engineered (Short YscP protein,YscP388: the spacer between the two export signals and one copy of the repeats in the central part are removed. Long YscP, yscP686: a restriction cleavage site between codons 250 and 251 in the central part of the yscP gene is engineered. A copy of codons 214-374, encoding the repeated region, into the restriction site is inserted). Genetic evidence is provided that only one molecule of YscP is required to control the length of one injectisome needle, thus supporting the static model of needle length regulation
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged truncation mutant enzymes from Escherichia coli strain BL21(DE3) are unfolded under denaturing conditions in 6 M guanidium-HCl, 25 mM Tris pH 8.0, 1 mM EDTA, 300 mM NaCl, followed by dialysis and refolding in 25 mM Tris, 50 mM NaCl
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
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glutathione S-transferase-enzyme fusion protein functions analogously to native protein. Overexpression of regulatory protein YscL impairs secretion
drug development
medicine
pilD-dependent mechanism for promoting Legionella pneumophila intracellular infection of human cells
pharmacology
drug development
the enzyme is a chemotherapeutic target for small-molecule ATPase inhibitors
drug development
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the enzyme is a chemotherapeutic target for small-molecule ATPase inhibitors
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pharmacology
the enzyme is a chemotherapeutic target for small-molecule ATPase inhibitors
pharmacology
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the enzyme is a chemotherapeutic target for small-molecule ATPase inhibitors
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