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Information on EC 7.4.2.5 - bacterial ABC-type protein transporter
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7.4.2.5 bacterial ABC-type protein transporterIUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. This entry stands for a family of bacterial enzymes that are dedicated to the secretion of one or several closely related proteins belonging to the toxin, protease and lipase families. Examples from Gram-negative bacteria include alpha-hemolysin, cyclolysin, colicin V and siderophores, while examples from Gram-positive bacteria include bacteriocin, subtilin, competence factor and pediocin.
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Word Map
- 7.4.2.5
-
caco-2
- tripeptides
- jejunum
-
gly-sar
-
glycylsarcosine
-
secyeg
- xenopus
- oocyte
-
histocompatibility
-
multidrug
-
prodrugs
- p-glycoprotein
-
enterocytes
- duodenum
-
peptidomimetic
- beta-lactams
- preproteins
-
basolateral
- ileum
- cephalexin
- laevis
-
peptide-like
-
translocons
-
transepithelial
-
brush-border
-
carrier-mediated
-
h+-coupled
-
villus
-
electrogenic
-
pepts
-
proton-dependent
- valacyclovir
- acyclovir
-
transporter-mediated
-
tapasin
- carnosine
-
sec-dependent
-
paracellular
-
membrane-embedded
-
two-electrode
- bestatin
- oct1
-
oatp2b1
-
oatps
-
antigen-processing
- gly-gly
- cefixime
-
i-restricted
-
apical-to-basolateral
-
serine-rich
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
pept1, peptide transporter, pept2, seca2, abc transport, seca protein, peptide transporter 1, abcb10, seca1, seca atpase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ABCB8
ABCB9
EC 3.6.3.43
-
-
formerly
-
H+/peptide cotransporter
HlyB
PepT1
PEPT2
peptide transporter
peptide transporter 1
peptide-transporting ATPase
PTR4
PTR6
SecA
SecA ATPase
SecA1
SecA1 ATPase
SecA2
SecA2 ATPase
TAP
TAPL
transporter associated with antigen processing-like
peptide-transporting ATPase
-
-
-
-
SecA2
transporter system component specializing in the cell-surface glycoprotein GspB
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + protein[side 1] = ADP + phosphate + protein[side 2]
ABC-type (ATP-binding cassette) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A family of enzymes which export alpha-hemolysin, cyclolysin, colicin V and sidophores from Gram-negative bacteria, and bacteriocin, subtilin, competence factor and pediocin from Gram-positive bacteria
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydolysis of phosphoric ester
-
-
-
-
hydrolysis of phosphoric ester
transmembrane transport
transmembrane transport
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, peptide-exporting)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. This entry stands for a family of bacterial enzymes that are dedicated to the secretion of one or several closely related proteins belonging to the toxin, protease and lipase families. Examples from Gram-negative bacteria include alpha-hemolysin, cyclolysin, colicin V and siderophores, while examples from Gram-positive bacteria include bacteriocin, subtilin, competence factor and pediocin.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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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
ATP + H2O + 5'-L-phenylalanyl-glycyl-floxuridine/in
ADP + phosphate + 5'-L-phenylalanyl-glycyl-floxuridine/out
-
-
-
-
?
ATP + H2O + beta-L-Ala-L-Lys-7-amido-4-methylcoumarin-3-acetic acid/in
ADP + phosphate + beta-L-Ala-L-Lys-7-amido-4-methylcoumarin-3-acetic acid/out
-
-
-
?
ATP + H2O + CRYQKSTEL/in
ADP + phosphate + CRYQKSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
ATP + H2O + Gly-L-His-Gly/in
ADP + phosphate + Gly-L-His-Gly/out
-
isoform PTR6
-
-
?
ATP + H2O + guanidine oseltamivir carboxylate-L-Val/in
ADP + phosphate + guanidine oseltamivir carboxylate-L-Val/out
ATP + H2O + hemoprotein HasA/in
ADP + phosphate + hemoprotein HasA/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
ATP + H2O + lacticin 481/in
ADP + phosphate + lacticin 481/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + lactococcin/in
ADP + phosphate + lactococcin/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
ATP + H2O + metalloprotease/in
ADP + phosphate + metalloprotease/out
-
metalloproteases PrtA,B,C,D
-
-
?
ATP + H2O + Msmeg1704/in
ADP + phosphate + Msmeg1704/out
-
-
-
ir
ATP + H2O + Msmeg1712/in
ADP + phosphate + Msmeg1712/out
-
-
-
ir
ATP + H2O + peptide/out
ADP + phosphate + peptide/in
-
ATP best substrate
-
-
?
ATP + H2O + pOA/in
ADP + phosphate + pOA/out
-
pOA, a truncated form of proOmpA with a new cysteine to allow for disulfide-loop formation
the disulfide-loop renders pOA unable to pass the channel, adding of DTT completes the translocation
-
ir
ATP + H2O + RCYQKSTEL/in
ADP + phosphate + RCYQKSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRCQKSTEL/in
ADP + phosphate + RRCQKSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQCSTEL/in
ADP + phosphate + RRYQCSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQKCTEL/in
ADP + phosphate + RRYQKCTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQKSCEL/in
ADP + phosphate + RRYQKSCEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQKSTCL/in
ADP + phosphate + RRYQKSTCL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQKSTEC/in
ADP + phosphate + RRYQKSTEC/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + TVDNKTRYR/in
ADP + phosphate + TVDNKTRYR/out
-
substrate in peptide transport assay, peptide is biotin-labeled at the lysine residue
-
-
?
CTP + H2O + peptide/out
CDP + phosphate + peptide/in
-
affinity for CTP is about 30fold lower compared to ATP
-
-
?
GTP + H2O + peptide/out
GDP + phosphate + peptide/in
-
affinity for GTP is about 30fold lower compared to ATP
-
-
?
UTP + H2O + peptide/out
UDP + phosphate + peptide/in
-
affinity for UTP is about 30fold lower compared to ATP
-
-
?
ATP + H2O
ADP + phosphate
-
ATP hydrolysis by SecA is required only if periplasmic loops larger than 30 amino acids have to be translocated. The signal recognition particle-dependent and SecA-dependent multiple spanning membrane protein YidC becomes SecA-independent if the large periplasmic loop connecting transmembrane domains 1 and 2 is reduced to less than 30 amino acids. The SecA dependence of a bacterial membrane protein is not solely determined by the length of the periplasmic loop but also by the presence of a down-stream TM domain
-
-
?
ATP + H2O
ADP + phosphate
-
ATPase SecA provides the driving force for the transport of secretory proteins across the cytoplasmic membrane of Escherichia coli
-
-
?
ATP + H2O
ADP + phosphate
-
SEcA drives a constant rate of preprotein translocation consistent with a stepping mechanism of translocation. The delay in full-length translocation for longer preproteins is dependent on the SecA motor function. The rate of protein translocation is controlled by the ATP concentration and is independent from the length of the preprotein
-
-
?
ATP + H2O
ADP + phosphate
-
SecB, a small cytosolic chaperone, captures the precursor polypeptides before they fold and delivers them to the membrane translocon through interactions with SecA. Both SecB and SecA display twofold symmetry and yet the complex between the two is stabilized by contacts that are distributed asymmetrically
-
-
?
ATP + H2O
ADP + phosphate
-
the preprotein binding domain is a preprotein receptor and a physical bridge connecting bound preproteins to the DEAD motor
-
-
?
ATP + H2O
ADP + phosphate
-
SecA2 plays a role in Mycobacterium tuberculosis inhibition of the immune response, which is likely important for survival in the host and pathogenesis
-
-
?
ATP + H2O + alpha-haemolysin/in
ADP + phosphate + alpha-haemolysin/out
-
-
-
-
?
ATP + H2O + alpha-haemolysin/in
ADP + phosphate + alpha-haemolysin/out
-
-
-
-
?
ATP + H2O + alpha-haemolysin/in
ADP + phosphate + alpha-haemolysin/out
-
-
-
-
?
ATP + H2O + cefadroxil/in
ADP + phosphate + cefadroxil/out
-
preferable substrate
-
-
?
ATP + H2O + cefadroxil/in
ADP + phosphate + cefadroxil/out
-
preferable substrate
-
-
?
ATP + H2O + cefadroxil/in
ADP + phosphate + cefadroxil/out
-
preferable substrate
-
-
?
ATP + H2O + D-phenylglycine-L-Dopa/in
ADP + phosphate + D-phenylglycine-L-Dopa/out
-
-
-
-
?
ATP + H2O + D-phenylglycine-L-Dopa/in
ADP + phosphate + D-phenylglycine-L-Dopa/out
-
-
-
-
?
ATP + H2O + D-phenylglycine-L-Dopa/in
ADP + phosphate + D-phenylglycine-L-Dopa/out
-
-
-
-
?
ATP + H2O + delta-aminolevulinic acid/in
ADP + phosphate + delta-aminolevulinic acid/out
-
-
-
-
?
ATP + H2O + delta-aminolevulinic acid/in
ADP + phosphate + delta-aminolevulinic acid/out
-
-
-
-
?
ATP + H2O + delta-aminolevulinic acid/in
ADP + phosphate + delta-aminolevulinic acid/out
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + glycyl-sarcosine/in
ADP + phosphate + glycyl-sarcosine/out
-
-
-
-
?
ATP + H2O + glycyl-sarcosine/in
ADP + phosphate + glycyl-sarcosine/out
-
-
-
-
?
ATP + H2O + glycyl-sarcosine/in
ADP + phosphate + glycyl-sarcosine/out
-
-
-
?
ATP + H2O + glycyl-sarcosine/in
ADP + phosphate + glycyl-sarcosine/out
-
-
-
-
?
ATP + H2O + glycyl-sarcosine/in
ADP + phosphate + glycyl-sarcosine/out
-
-
-
?
ATP + H2O + guanidine oseltamivir carboxylate-L-Val/in
ADP + phosphate + guanidine oseltamivir carboxylate-L-Val/out
-
-
-
-
?
ATP + H2O + guanidine oseltamivir carboxylate-L-Val/in
ADP + phosphate + guanidine oseltamivir carboxylate-L-Val/out
-
-
-
-
?
ATP + H2O + guanidine oseltamivir carboxylate-L-Val/in
ADP + phosphate + guanidine oseltamivir carboxylate-L-Val/out
-
-
-
-
?
ATP + H2O + JBP485/in
ADP + phosphate + JBP485/out
-
JBP485 is cyclo-trans-4-L-hydroxyprolyl-L-serine
-
-
?
ATP + H2O + JBP485/in
ADP + phosphate + JBP485/out
-
JBP485 is cyclo-trans-4-L-hydroxyprolyl-L-serine
-
-
?
ATP + H2O + JBP485/in
ADP + phosphate + JBP485/out
-
JBP485 is cyclo-trans-4-L-hydroxyprolyl-L-serine
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + L-Ala-L-Ala/in
ADP + phosphate + L-Ala-L-Ala/out
K0.5 value 0.023 mM at -140 mV
-
-
?
ATP + H2O + L-Ala-L-Ala/in
ADP + phosphate + L-Ala-L-Ala/out
K0.5 value 0.057 mM at -140 mV
-
-
?
ATP + H2O + L-Ala-L-Asp/in
ADP + phosphate + L-Ala-L-Asp/out
K0.5 value 0.058 mM at -140 mV
-
-
?
ATP + H2O + L-Ala-L-Asp/in
ADP + phosphate + L-Ala-L-Asp/out
K0.5 value 0.129 mM at -140 mV
-
-
?
ATP + H2O + L-Ala-L-Lys/in
ADP + phosphate + L-Ala-L-Lys/out
K0.5 value 0.142 mM at -140 mV
-
-
?
ATP + H2O + L-Ala-L-Lys/in
ADP + phosphate + L-Ala-L-Lys/out
K0.5 value 0.167 mM at -140 mV
-
-
?
ATP + H2O + L-Val-didanosine/in
ADP + phosphate + L-Val-didanosine/out
-
didanosine is also named Videx or 5'-O-2'-3'-dideoxydidanosine
-
-
?
ATP + H2O + L-Val-didanosine/in
ADP + phosphate + L-Val-didanosine/out
-
didanosine is also named Videx or 5'-O-2'-3'-dideoxydidanosine
-
-
?
ATP + H2O + L-Val-didanosine/in
ADP + phosphate + L-Val-didanosine/out
-
didanosine is also named Videx or 5'-O-2'-3'-dideoxydidanosine
-
-
?
ATP + H2O + lactococcin G/in
ADP + phosphate + lactococcin G/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + lactococcin G/in
ADP + phosphate + lactococcin G/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + Msmeg1704 in
ADP + phosphate + Msmeg1704 out
-
-
-
ir
ATP + H2O + Msmeg1704 in
ADP + phosphate + Msmeg1704 out
-
-
-
ir
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + NP-647/in
ADP + phosphate + NP-647/out
-
NP-647 is L-pGlu-(2-propyl)-L-His-L-ProNH2
-
-
?
ATP + H2O + NP-647/in
ADP + phosphate + NP-647/out
-
NP-647 is L-pGlu-(2-propyl)-L-His-L-ProNH2
-
-
?
ATP + H2O + NP-647/in
ADP + phosphate + NP-647/out
-
NP-647 is L-pGlu-(2-propyl)-L-His-L-ProNH2
-
-
?
ATP + H2O + oseltamivir carboxylate/in
ADP + phosphate + oseltamivir carboxylate/out
-
the enzyme is not implicated in the oral absorption of oseltamivir carboxylate
-
-
?
ATP + H2O + oseltamivir carboxylate/in
ADP + phosphate + oseltamivir carboxylate/out
-
the enzyme is not implicated in the oral absorption of oseltamivir carboxylate
-
-
?
ATP + H2O + oseltamivir/in
ADP + phosphate + oseltamivir/out
-
the enzyme is not implicated in the oral absorption of oseltamivir
-
-
?
ATP + H2O + oseltamivir/in
ADP + phosphate + oseltamivir/out
-
the enzyme is not implicated in the oral absorption of oseltamivir
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
TAPL is a half-type ABC transporter that localizes in lysosome and putatively conveys peptides from cytosol to lysosome
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
the enzyme translocates cytosolic peptides into the lumen of lysosomes driven by the hydrolysis of ATP
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + RRYCKSTEL/in
ADP + phosphate + RRYCKSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYCKSTEL/in
ADP + phosphate + RRYCKSTEL/out
-
substrate in peptide transport assay, fluorescein coupled via a cyteine residue
-
-
?
ATP + H2O + RRYQNSTCL/in
ADP + phosphate + RRYQNSTCL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQNSTCL/in
ADP + phosphate + RRYQNSTCL/out
-
substrate in peptide transport assay, fluorescein coupled via a cyteine residue
-
-
?
ATP + H2O + subtilisin/in
ADP + phosphate + subtilisin/out
-
-
-
-
?
additional information
?
-
dipeptide transport by AtPTR1 is electrogenic and dependent on protons but not sodium. Transport activity is voltage-dependent, and currents increase supralinearly with more negative membrane potentials and do not saturate. The voltage dependence of the apparent affinities differes between Ala-Ala, Ala-Lys, and Ala-Asp and is not conserved between the two transporters AtPTR1 and AtPTR5. The apparent affinity of AtPTR1 for these dipeptides is pH-dependent and decreases with decreasing proton concentration
-
-
?
additional information
?
-
dipeptide transport by AtPTR1 is electrogenic and dependent on protons but not sodium. Transport activity is voltage-dependent, and currents increase supralinearly with more negative membrane potentials and do not saturate. The voltage dependence of the apparent affinities differes between Ala-Ala, Ala-Lys, and Ala-Asp and is not conserved between the two transporters AtPTR1 and AtPTR5. The apparent affinity of AtPTR1 for these dipeptides is pH-dependent and decreases with decreasing proton concentration
-
-
?
additional information
?
-
dipeptide transport by AtPTR5 is electrogenic and dependent on protons but not sodium. Transport activity is voltage-dependent, and currents increase supralinearly with more negative membrane potentials and do not saturate. The voltage dependence of the apparent affinities differes between Ala-Ala, Ala-Lys, and Ala-Asp and is not conserved between the two transporters AtPTR1 and AtPTR5
-
-
?
additional information
?
-
dipeptide transport by AtPTR5 is electrogenic and dependent on protons but not sodium. Transport activity is voltage-dependent, and currents increase supralinearly with more negative membrane potentials and do not saturate. The voltage dependence of the apparent affinities differes between Ala-Ala, Ala-Lys, and Ala-Asp and is not conserved between the two transporters AtPTR1 and AtPTR5
-
-
?
additional information
?
-
no substrate: His-Ala, Ala-Ala, Ala-Lys, Ala-Asp
-
-
?
additional information
?
-
no substrate: His-Ala, Ala-Ala, Ala-Lys, Ala-Asp
-
-
?
additional information
?
-
-
Caenorhabditis elegans requires ABC transporters HAF-4 and HAF-9, which are highly homologous to human lysosomal peptide transporter TAPL
-
-
?
additional information
?
-
-
one intact nucleotide-binding domain within a dimer is sufficient for ATP hydrolysis. One ATP-binding site of the dimer is able to function independently of the hydrolytic capability of the neighboring ATP-binding site. Sequential mechanism of ATP hydrolysis in the intact HlyB transporter
-
-
?
additional information
?
-
-
ATPase activity associated with transporter associated with antigen processing, TAP. Role of TAP in peptide loading of MHC molecules and the overall process of antigen presentation
-
-
?
additional information
?
-
-
coordinated dialogue between peptide binding site, nucleotide-binding domain, and the translocation site
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
the enzyme binds ATP, ADP, GTP, and dATP, UTP, and CTP to a lower extent, but not AMP
-
-
?
additional information
?
-
-
permeation of cationic antimicrobial di- and tripeptides derived from lactoferricin and test for interaction with PEPT1, none serves as a substrate
-
-
?
additional information
?
-
-
using the two-electrode, voltage-clamp technique at Xenopus laevis oocytes, strong hPEPT1-specific inward transport currents are recorded for glycylsarcosine, anserine and carnosine, but not for glycine
-
-
?
additional information
?
-
-
isoform PTR6 shows substrate selectivity for di- and tripeptides
-
-
?
additional information
?
-
-
the enzyme binds ATP, ADP, GTP, and dATP, UTP, and CTP to a lower extent, but not AMP
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
ATP + H2O + hemoprotein HasA/in
ADP + phosphate + hemoprotein HasA/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
ATP + H2O + lacticin 481/in
ADP + phosphate + lacticin 481/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + lactococcin/in
ADP + phosphate + lactococcin/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
ATP + H2O + metalloprotease/in
ADP + phosphate + metalloprotease/out
-
metalloproteases PrtA,B,C,D
-
-
?
ATP + H2O + Msmeg1704/in
ADP + phosphate + Msmeg1704/out
-
-
-
ir
ATP + H2O + Msmeg1712/in
ADP + phosphate + Msmeg1712/out
-
-
-
ir
ATP + H2O
ADP + phosphate
-
ATP hydrolysis by SecA is required only if periplasmic loops larger than 30 amino acids have to be translocated. The signal recognition particle-dependent and SecA-dependent multiple spanning membrane protein YidC becomes SecA-independent if the large periplasmic loop connecting transmembrane domains 1 and 2 is reduced to less than 30 amino acids. The SecA dependence of a bacterial membrane protein is not solely determined by the length of the periplasmic loop but also by the presence of a down-stream TM domain
-
-
?
ATP + H2O
ADP + phosphate
-
ATPase SecA provides the driving force for the transport of secretory proteins across the cytoplasmic membrane of Escherichia coli
-
-
?
ATP + H2O
ADP + phosphate
-
SecA2 plays a role in Mycobacterium tuberculosis inhibition of the immune response, which is likely important for survival in the host and pathogenesis
-
-
?
ATP + H2O + alpha-haemolysin/in
ADP + phosphate + alpha-haemolysin/out
-
-
-
-
?
ATP + H2O + alpha-haemolysin/in
ADP + phosphate + alpha-haemolysin/out
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + lactococcin G/in
ADP + phosphate + lactococcin G/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + lactococcin G/in
ADP + phosphate + lactococcin G/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + Msmeg1704 in
ADP + phosphate + Msmeg1704 out
-
-
-
ir
ATP + H2O + Msmeg1704 in
ADP + phosphate + Msmeg1704 out
-
-
-
ir
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
TAPL is a half-type ABC transporter that localizes in lysosome and putatively conveys peptides from cytosol to lysosome
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
the enzyme translocates cytosolic peptides into the lumen of lysosomes driven by the hydrolysis of ATP
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + subtilisin/in
ADP + phosphate + subtilisin/out
-
-
-
-
?
additional information
?
-
-
Caenorhabditis elegans requires ABC transporters HAF-4 and HAF-9, which are highly homologous to human lysosomal peptide transporter TAPL
-
-
?
additional information
?
-
-
ATPase activity associated with transporter associated with antigen processing, TAP. Role of TAP in peptide loading of MHC molecules and the overall process of antigen presentation
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
ATP hydrolysis activity of the recombinant protein 6His-SecA is highest with 0.1 mM Mg2+ and decreases both with higher and lower concentration of Mg2+
Mg2+
ATP hydrolysis activity of the recombinant protein 6His-SecA2 aquires at least 0.5 mM Mg2+ and is higher with 2.5 mM Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(4-bromophenyl)-5-cyano-4-oxopyrimidine)
-
-
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(biphenyl-4-yl)-5-cyano-4-oxopyrimidine)
-
compound does not show antimicrobial activity
2-((4-azidobenzyl)thio)-4-(4-(benzyloxy)phenyl)-6-oxo-1,6-dihydropyrimidine-5-carbonitrile
good antimicrobial inhibition with MIC of 12.5 microM
2-((4-azidobenzyl)thio)-6-oxo-4-(4-phenoxyphenyl)-1,6-dihydropyrimidine-5-carbonitrile
good antimicrobial inhibition with MIC of 18.2 microM
2-(benzylsulfanyl)-4-(biphenyl-4-yl)-6-oxo-1,6-dihydropyrimidine-5-carbonitrile
-
exhibits most potent inhibition effects against strain NR698 with increased outer membrane permeability
3-biphenyl-L-alanyl-L-arginine methyl ester
-
peptide derived from lactoferricin, at 1 mM, 10% inhibition of glycylsarcosine-induced current
azide
1.5 mM azide decrease the transport of the cell-surface glycoprotein mutant GspB736flag, 15 mM nearly prevent transport of GspB736flag, azide have no effect on ATP hydrolysis activity of the recombinant protein 6His-SecA; 1.5 mM azide markedly decrease the transport of the cell-surface glycoprotein mutant GspB736flag, 15 mM nearly prevent transport of GspB736flag, azide have no effect on ATP hydrolysis activity of the recombinant protein 6His-SecA2
Carbonyl cyanide m-chlorophenylhydrazone
10 mM, 20% residual activity; 10 mM, 26% residual activity
cisplatin
-
IC50 value for growth inhibition of cell line PC-3 0.0033 mM, DU-145 0.0045 mM, 2008 0.0194 mM, C-13 0.117 mM, L-540 0.0025 mM
diethyl dicarbonate
10 mM, 0.4% residual activity; 10 mM, 0.6% residual activity
erythrosin B
-
the potency in inhibiting the truncated SecA ATPase correlates with the ability to inhibit the biologically relevant protein translocation activity of SecA and also translates into antibacterial effects
Fv fragment of the monoclonal antibody mAb148.3
-
Fv binding to the C terminus of TAP1
-
L-Phe-L-Ala
in the absence of dipeptides, transporter shows proton-dependent leak currents that are inhibited by Phe-Ala; in the absence of dipeptides, transporter shows proton-dependent leak currents that are inhibited by Phe-Ala, Trp-Ala, and Phe-Phe
L-Phe-L-Phe
in the absence of dipeptides, transporter shows proton-dependent leak currents that are inhibited by Phe-Ala, Trp-Ala, and Phe-Phe. Phe-Ala reduces leak currents by binding to the substrate-binding site with a high apparent affinity
L-Trp-L-Ala
in the absence of dipeptides, transporter shows proton-dependent leak currents that are inhibited by Phe-Ala, Trp-Ala, and Phe-Phe
N-ethylmaleimide
10 mM, 12% residual activity; 10 mM, 14% residual activity
Rose bengal
-
the potency in inhibiting the truncated SecA ATPase correlates with the ability to inhibit the biologically relevant protein translocation activity of SecA and also translates into antibacterial effects
RWR-NH(benzyl)
-
peptide derived from lactoferricin, at 1 mM, 87% inhibition of glycylsarcosine-induced current, peptide can also impair membrane protein functions in an unspecific manner
RWR-NH2
-
peptide derived from lactoferricin, at 1 mM, 15% inhibition of glycylsarcosine-induced current
[AuIIIBr2(dtc-Sar-Aib-O(t-Bu))]
-
IC50 value for growth inhibition of cell line PC-3 0.0008 mM, DU-145 0.0014 mM, 2008 0.0045 mM, C-13 0.0037 mM, L-540 0.0015 mM
[AuIIICl2(dtc-Sar-Aib-O(t-Bu))]
-
IC50 value for growth inhibition of cell line PC-3 0.0011 mM, DU-145 0.0022 mM, 2008 0.0047 mM, C-13 0.0051 mM, L-540 0.0017 mM
additional information
-
Insertion of charged amino acid residues into the preprotein proOmpA strongly inhibits SecA translocation ATPase activity. Stretches of positively charged residues are much stronger translocation inhibitors and suppressors of the preprotein-stimulated SecA ATPase activity than negatively charged residues.
-
Mg2+
-
2 mM Mg2+ blocks SecA ATPase activity almost completely, the inhibition is abolishable by binding of SecA to the protein channel SecYEG in proteoliposomes (1 micromol)
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Calcium
-
27-82 micromol Ca2+ enhances ATPase activity in presence of Escherichia coli PE/anionic phospholipid membranes up to 3-fold
DTT
effect on mutant N95CC, a large stimulation of ATPase activity is only observed when both proOmpA and DTT are present
Phospholipid
-
stimulated up to 4fold by phospholipids with an optimum at 74°C. Membrane vesicles and proteoliposomes containing SecYE and SecYEG support 2fold to 4fold stimulation of the precursor dependent SecA ATPase activity
proOmpA
effect on mutant N95CC, a large stimulation of ATPase activity is only observed when both proOmpA and DTT are present
-
SecM
-
SecA synthesized without the signal sequence on SecM is much less active on average than that synthesized in combination with normal SecM. The elongation arrest per se is not sufficient in terms of the SecA-activating ability of SecM. Targeting of nascent SecM to the membrane translocon is another crucial feature for SecM to enhance SEcA activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
ATP hydrolysis rate 10.5 nmol phosphate/min/nmol SecA1
-
additional information
additional information
ATP hydrolysis rate 10.5 nmol phosphate/min/nmol SecA1
-
additional information
additional information
-
ATP hydrolysis rate 10.5 nmol phosphate/min/nmol SecA1
-
additional information
additional information
ATP hydrolysis rate SecA wild-type 6.1 nmol phosphate/min/nmol enzyme
-
additional information
additional information
-
ATP hydrolysis rate SecA wild-type 6.1 nmol phosphate/min/nmol enzyme
-
additional information
additional information
ATP hydrolysis rate SecA2 wild-type 19.7, K115R mutant 25.0, K115A mutant 13.5 nmol Pi/min/nmol enzyme
-
additional information
additional information
ATP hydrolysis rate SecA2 wild-type 19.7, K115R mutant 25.0, K115A mutant 13.5 nmol Pi/min/nmol enzyme
-
additional information
additional information
-
ATP hydrolysis rate SecA2 wild-type 19.7, K115R mutant 25.0, K115A mutant 13.5 nmol Pi/min/nmol enzyme
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
alafosfalin
mutant K274I, pH 7.5, temperature not specified in the publication
0.07
alafosfalin
wild-type, pH 7.5, temperature not specified in the publication
0.25
alafosfalin
mutant M154K, pH 7.5, temperature not specified in the publication
0.28
alafosfalin
mutant V252E, pH 7.5, temperature not specified in the publication
0.38
alafosfalin
mutant L190V, pH 7.5, temperature not specified in the publication
0.45
alafosfalin
mutant F197I, pH 7.5, temperature not specified in the publication
0.96
alafosfalin
mutant L324V, pH 7.5, temperature not specified in the publication
0.08
L-Ala-L-Ala
mutant M154K, pH 7.5, temperature not specified in the publication
0.2
L-Ala-L-Ala
mutant K274I, pH 7.5, temperature not specified in the publication
0.2
L-Ala-L-Ala
mutant L190V, pH 7.5, temperature not specified in the publication
0.21
L-Ala-L-Ala
mutant V252E, pH 7.5, temperature not specified in the publication
0.21
L-Ala-L-Ala
wild-type, pH 7.5, temperature not specified in the publication
0.31
L-Ala-L-Ala
mutant F197I, pH 7.5, temperature not specified in the publication
0.36
L-Ala-L-Ala
mutant L324V, pH 7.5, temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002 - 0.02
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(4-bromophenyl)-5-cyano-4-oxopyrimidine)
0.002 - 0.05
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(biphenyl-4-yl)-5-cyano-4-oxopyrimidine)
0.0024
2-((4-azidobenzyl)thio)-4-(4-(benzyloxy)phenyl)-6-oxo-1,6-dihydropyrimidine-5-carbonitrile
Escherichia coli
37°C, pH not specified in the publication
0.0022
2-((4-azidobenzyl)thio)-6-oxo-4-(4-phenoxyphenyl)-1,6-dihydropyrimidine-5-carbonitrile
Escherichia coli
37°C, pH not specified in the publication
0.06
2-(benzylsulfanyl)-4-(biphenyl-4-yl)-6-oxo-1,6-dihydropyrimidine-5-carbonitrile
Escherichia coli
-
recombinant SecA, pH 7.6, 40°C
0.025
eosin Y
Escherichia coli
-
truncated SecA without the C-terminal regulatory domain, 40°C, pH 7.6
0.002
erythrosin B
Escherichia coli
-
truncated SecA without the C-terminal regulatory domain, 40°C, pH 7.6
0.0005
Rose bengal
Escherichia coli
-
truncated SecA without the C-terminal regulatory domain, pH 7.6, 40°C
0.002
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(4-bromophenyl)-5-cyano-4-oxopyrimidine)
Escherichia coli
-
EcN68, the N-terminal fragment of SecA without the C-terminal regulatory domain, pH 7.6, 40°C
0.02
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(4-bromophenyl)-5-cyano-4-oxopyrimidine)
Escherichia coli
-
recombinant SecA, pH 7.6, 40°C
0.002
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(biphenyl-4-yl)-5-cyano-4-oxopyrimidine)
Escherichia coli
-
EcN68, the N-terminal fragment of SecA without the C-terminal regulatory domain, pH 7.6, 40°C
0.05
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(biphenyl-4-yl)-5-cyano-4-oxopyrimidine)
Escherichia coli
-
recombinant SecA, pH 7.6, 40°C
0.08
alafosfalin
Escherichia coli
mutant K274I, pH 7.5, temperature not specified in the publication
0.11
alafosfalin
Escherichia coli
wild-type, pH 7.5, temperature not specified in the publication
0.39
alafosfalin
Escherichia coli
mutant M154K, pH 7.5, temperature not specified in the publication
0.44
alafosfalin
Escherichia coli
mutant V252E, pH 7.5, temperature not specified in the publication
0.59
alafosfalin
Escherichia coli
mutant L190V, pH 7.5, temperature not specified in the publication
0.71
alafosfalin
Escherichia coli
mutant F197I, pH 7.5, temperature not specified in the publication
1.5
alafosfalin
Escherichia coli
mutant L324V, pH 7.5, temperature not specified in the publication
0.12
L-Ala-L-Ala
Escherichia coli
mutant M154K, pH 7.5, temperature not specified in the publication
0.31
L-Ala-L-Ala
Escherichia coli
mutant K274I, pH 7.5, temperature not specified in the publication
0.32
L-Ala-L-Ala
Escherichia coli
mutant L190V, pH 7.5, temperature not specified in the publication
0.33
L-Ala-L-Ala
Escherichia coli
mutant V252E, pH 7.5, temperature not specified in the publication
0.33
L-Ala-L-Ala
Escherichia coli
wild-type, pH 7.5, temperature not specified in the publication
0.48
L-Ala-L-Ala
Escherichia coli
mutant F197I, pH 7.5, temperature not specified in the publication
0.56
L-Ala-L-Ala
Escherichia coli
mutant L324V, pH 7.5, temperature not specified in the publication
additional information
beta-Ala-Lys
Escherichia coli
IC50 value range between 0.1 and 1 mM for wild-type and E20-mutants, and increase to above 10 mM for mutant E388Q, pH not specified in the publication, temperature not specified in the publication
additional information
beta-Ala-Lys
Escherichia coli
-
IC50 value range between 0.1 and 1 mM for wild-type and E20-mutants, and increase to above 10 mM for mutant E388Q, pH not specified in the publication, temperature not specified in the publication
additional information
Gly-Lys
Escherichia coli
IC50 value range between 0.1 and 1 mM for wild-type and E20-mutants, and increase to about 2 mM for mutant E388Q, pH not specified in the publication, temperature not specified in the publication
additional information
Gly-Lys
Escherichia coli
-
IC50 value range between 0.1 and 1 mM for wild-type and E20-mutants, and increase to about 2 mM for mutant E388Q, pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00000022
0.00000026
0.0000003
-
peptide transport rate, K545A/H699A mutant, in the presence of 3 mM ATP and 1 mM orthovanadate
0.00000035
-
peptide transport rate, wild type, in the presence of 3 mM ATP and 500 microM competitor peptide RRYQKSTEL
0.00000039
-
peptide transport rate, K545A/H699A mutant, in the presence of 3 mM AMP
0.000003
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, DOPC-eggPG, 9 to 1
0.000004
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, DOPC-DOPE, 9 to 1
0.000006
-
peptide transport rate, TAPL reconstituted in liposomes prepared from bovine heart lipids
0.000011
-
peptide transport rate, TAPL reconstituted in liposomes prepared from bovine brain lipids
0.000023
-
peptide transport rate, TAPL reconstituted in liposomes prepared from bovine liver lipids
0.000045
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 100% phosphatidylcholine
0.00007
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 90% DOPS
0.000075
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, DOPC-DOPA, 9 to 1
0.000095
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 10% DOPS
0.000115
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 70% phosphatidylcholine
0.000135
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, DOPC-DOPS, 9 to 1
0.000245
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 70% DOPS
0.00026
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 30% DOPS
0.00042
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids
0.000423
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 50% DOPS
0.000505
-
peptide transport rate, TAPL reconstitution in Eschericha coli liposomes, for comparison
0.000535
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, for comparison in Eschericha coli liposomes
0.00055
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, no phosphatidylcholine
0.00127
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 50% phosphatidylcholine
0.00132
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 10% phosphatidylcholine
0.00168
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 30% phosphatidylcholine
0.0065
additional information
0.00000022
-
peptide transport rate, K545A/H699A mutant, in the presence of 3 mM ATP
0.00000022
-
peptide transport rate, wild type, in the presence of 3 mM ATP and 1 mM orthovanadate
0.00000026
-
peptide transport rate, K545A/H699A mutant, in the presence of 3 mM ATP and 500 microM competitor peptide RRYQKSTEL
additional information
-
10 nM Pi/min/nM SecA in presence of Escherichia coli PE/anionic phospholipid membranes
additional information
-
425 mol ATP/min/mol SecA in presence of 0.2 micromol preprotein translocation substrate proOmpA in urea
additional information
-
in ATPase translocation activity assay with preprotein translocation substrate proOmpA: circa 0.8 mM ATP/2 micromol SecA after 1 min, mutant SecA proteins with deletions of amino acids between 2-11 shows ATPase translocation activity around 0.25 mM ATP/2 micromol SecA after 1 min
additional information
-
translocation ATPase activity: 0.9 nmol phosphate/microgramm SecA/min, mutants lacking 2 to 11 residues of the amino terminus of SecA shows defect translocation ATPase activities (below 0.1 nmol phosphate/microgramm/min)
additional information
circa 1.8 pMol Pi/pMol 6His-SecA2/min, measured in an assay containing 2.5 mM Mg2+
additional information
circa 1.8 pMol Pi/pMol 6His-SecA2/min, measured in an assay containing 2.5 mM Mg2+
additional information
-
circa 1.8 pMol Pi/pMol 6His-SecA2/min, measured in an assay containing 2.5 mM Mg2+
additional information
circa 7 pMol phosphate/pMol 6His-SecA/min measured in an assay containing 0.1 mM Mg2+
additional information
circa 7 pMol phosphate/pMol 6His-SecA/min measured in an assay containing 0.1 mM Mg2+
additional information
-
circa 7 pMol phosphate/pMol 6His-SecA/min measured in an assay containing 0.1 mM Mg2+
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.5
-
pH 7.0: about 75% of maximal activity, pH 8.5: about 85% of maximal activity
additional information
additional information
an increased luminal pH results in decreased intestinal dipeptide transport in freshwater-acclimated fish
additional information
-
an increased luminal pH results in decreased intestinal dipeptide transport in freshwater-acclimated fish
additional information
an increased luminal pH results in decreased intestinal dipeptide transport in freshwater-acclimated fish but suggests an increased dipeptide transport in seawater-acclimated fish
additional information
-
an increased luminal pH results in decreased intestinal dipeptide transport in freshwater-acclimated fish but suggests an increased dipeptide transport in seawater-acclimated fish
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC13032 (wild-type) and strain CgdeltasecA1 (pVA1) containing the secA1-his6 gene on a plasmid
UniProt
brenda
strain ATCC13032 (wild-type) and strain CgdeltasecA2 (pVA2) containing the secA2-his6 gene on a plasmid
UniProt
brenda
-
210372, 210376, 210379, 667495, 667693, 668736, 669390, 669401, 669417, 669429, 669458, 670687, 670832
-
-
brenda
-
686718, 687520, 687533, 687663, 687726, 688357, 700101, 700137, 710640, 719456, 720188, 720196, 720918, 733062, 733688, 733708
-
-
brenda
ATPase activity associated with transporter associated with antigen processing, TAP
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
TAPL expression is strongly induced during differentiation of monocytes to dendritic cells and to macrophages
brenda
-
in grain-filling seeds, expression of isoforms OsPTR4, OsPTR7 and OsPTR8 increases from early to late stages of seed development and that of OsPTR2, OsPTR3 and OsPTR6 decreases
brenda
-
human TAP-deficient lymphoblastoid cell, expressing rat wild-type TAP or single rat TAP1 or TAP2 chains
brenda
additional information
-
tissue-specific expression of genes haf-4 and haf-9: both recombinant GFP-tagged HAF-4 and HAF-9 are mainly localized on the membrane of non-acidic but LAMP homologue-positive intestinal granules from larval to adult stage
brenda
additional information
not detected in brain, heart, gill, liver. esophagus, stomach, rectum, head kidney, body kidney, urinary bladder, and muscle
brenda
additional information
-
not detected in brain, heart, gill, liver. esophagus, stomach, rectum, head kidney, body kidney, urinary bladder, and muscle
brenda
additional information
expression both in seawater- and freshwater-acclimated fish
brenda
additional information
-
expression both in seawater- and freshwater-acclimated fish
brenda
additional information
expression only in seawater-acclimated fish
brenda
additional information
-
expression only in seawater-acclimated fish
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
SecA-dependent secretion and SrtA anchoring machineries are spatially coupled and localized at the division septum in exponentially growing cultures
brenda
-
brenda
-
inner membrane detected by immunoblotting, ExeA, cytoplasmic domain with ATP-binding site
brenda
-
SpaF, ATP-binding protein, membrane spanning domain located at C-terminus
brenda
-
TAP1 and TAP2, hydrophobic N-terminus, C-terminal ABC domain
brenda
-
LctE and LctG transmembrane domains, Lctf ATP-binding domain
brenda
-
LcnC, N- and C-terminal parts located in the cytoplasm
brenda
-
TAP1 and TAP2, hydrophobic N-terminus, C-terminal ABC domain
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme ablation results in 3-5fold reduction in the in vivo rate and extent of valacyclovir absorption
physiological function
physiological function
-
Both SecA and the ribosome need to interact with the translocon during membrane protein insertion. SecA and ribosome binding to the translocon is mutually exclusive, implying that during membrane protein insertion, both ligands bind the translocon in a sequential manner
physiological function
-
mechanism of Sap-mediated import of antimicrobial peptides, a strategy to reduce periplasmic and inner membrane accumulation of these host defense peptides. Antimicrobial peptides localize to the bacterial cytoplasm of the wild-type strain and are susceptible to cytoplasmic peptidase activity. In bacteria lacking a functional Sap permease complex, antimicrobial peptides accumulate in the periplasm. The periplasmic binding protein SapA binds antimicrobial peptides and is required for virulence in vivo
physiological function
-
multiple SecA molecules drive translocation across a single translocon with SecG inversion. Model of proOmpA translocation suggests that a single catalytic cycle of SecA causes translocation of 1013 kDa with ATP binding and hydrolysis, and SecG inversion is required when the next SecA cycle begins with additional ATP hydrolysis
physiological function
-
SecA ATPase associates with the SecY complex to push preproteins across the bacterial membrane. One SecY copy is sufficient to bind SecA and the preprotein, but only the SecY dimer together with acidic lipids supports the activation of the SecA translocation ATPase. In nanodiscs, the dimer is predominantly arranged in a back-to-back manner and remains active even if a constituent SecY copy is defective for SecA binding. In membrane vesicles and in intact cells, the coproduction of two inactive SecYs, one for channel gating and the other for SecA binding, recreates a functional translocation unit
physiological function
-
Similarly to a SecA2 deletion mutant, a SecA2 ATPase bearing a mutated nucleotide binding site exhibits rough colonies, a bacterial chaining phenotype, an impaired protein secretion profile, and in vivo virulence in comparison to wild-type Listeria monocytogenes. Mice immunized with the SecA2 nucelotide binding site mutant are not protected against secondary infection with wild-type Listeria monocytogenes and do not develop CCL3+ memory CD8+ T cells
physiological function
role for the SecA2 pathway in the cell wall localization of solute binding proteins that work with ABC transporters to import solutes. Additionally, SecA2 has a profound effect on the cell wall localization of the Mce1 and Mce4 lipid transporters, which contribute to Mycobacterium tuberculosis virulence. A relationship exists between SecA2 and the hypoxia-induced DosR regulon associated with Mycobacterium tuberculosis latency. Nearly half of the transcriptionally controlled DosR regulon of cytoplasmic proteins are detected at higher levels in the secA2 mutant versus wild-type
physiological function
-
the enzyme contributes to water absorption in the colon
physiological function
-
the enzyme contributes to water absorption in the colon
physiological function
-
the enzyme contributes to water absorption in the colon
physiological function
-
role for the SecA2 pathway in the cell wall localization of solute binding proteins that work with ABC transporters to import solutes. Additionally, SecA2 has a profound effect on the cell wall localization of the Mce1 and Mce4 lipid transporters, which contribute to Mycobacterium tuberculosis virulence. A relationship exists between SecA2 and the hypoxia-induced DosR regulon associated with Mycobacterium tuberculosis latency. Nearly half of the transcriptionally controlled DosR regulon of cytoplasmic proteins are detected at higher levels in the secA2 mutant versus wild-type
-
physiological function
-
Both SecA and the ribosome need to interact with the translocon during membrane protein insertion. SecA and ribosome binding to the translocon is mutually exclusive, implying that during membrane protein insertion, both ligands bind the translocon in a sequential manner
-
Show AA Sequence and Transmembrane Helices (949 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
102000
106000
monomer, predicted molecular mass, determined by SDS-PAGE
109000
Streptococcus parasanguis strain VT1700, expressed from plasmid, deletion mutant, residues 590-676 are deleted, GFP-tag, 86.8% in the membrane
200000
54000
Streptococcus parasanguis strain VT1697, expressed from plasmid, deletion mutant, residues 1-330 are deleted
64000
65000
Streptococcus parasanguis strain VT1694, expressed from plasmid, deletion mutant, residues 578-797 are deleted, 76.6% in the membrane
66000
-
gel filtration in presence of MgATP2- and BeFx or orthovanadate
70000
72000
79000
Streptococcus parasanguis strain VT1584, expressed from plasmid, deletion mutant, residues 678-779 are deleted, 68.0% in the membrane
81000
82000
Streptococcus parasanguis strain VT1702, expressed from plasmid, deletion muatnt, 1-330 are deleted, GFP-tag, 84.4% in the membrane
85400
monomer, predicted molecular mass, determined by SDS-PAGE
92000
97000
102000
2 * 102000, gel filtration, furthermore electron paramagnetic resonance spectroscopy used to identify the interactive binding surface of SecA
200000
-
molecular weight depends on dimerization rate which depends on concentration of SecA and KCl: at 100 nM KCl molecular weight is 200000 Da, at 300 nM KCl molecular weight is around 140000 Da (both at 1microM SecA), monomer-dimer equilibrium is altered in SecA mutants: mutants lacking 2 to 11 residues of the amino terminus of SecA failed to form dimers at 1microM SecA and 300 nM KCl, determination by gel filtration controlling eluate by photodiode array UV/Vis detector, a differential refractometer and a static, multiangle laser light scattering detector
64000
Streptococcus parasanguis strain VT1574, expressed from chromosomal locus, deletion mutant, residues 331-583 are deleted, 83.6% in the membrane
64000
Streptococcus parasanguis strain VT1584, expressed from chromosomal locus, deletion mutant
81000
Streptococcus parasanguis strain VT1583, expressed from chromosomal locus, deletion mutant, residues 590-676 are deleted
81000
Streptococcus parasanguis strain VT1700, expressed from chromosomal locus, deletion mutant, residues 590-676 are deleted
81000
Streptococcus parasanguis strain VT1702, expressed from chromosomal locus, deletion mutant, residues 590-676 are deleted
92000
Streptococcus parasanguis strain FW213, expressed from chromosomal locus, full-length protein, 95.5% in the membrane
92000
Streptococcus parasanguis strain VT1694, expressed from chromosomal locus, full-length protein
92000
Streptococcus parasanguis strain VT1697, expressed from chromosomal locus, full-length protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
homodimer
monomer
additional information
dimer
-
is the active form of the enzyme. ATP-promoted dimerization of HlyB-nucleotide binding domain might involve formation of two interconvertible forms: a readily dissociable active dimer and a more stable, reversibly inactive form of the dimer
dimer
-
membrane-bound SEcA dimer exists and is required for effective protein translocation
dimer
2 * 102000, gel filtration, furthermore electron paramagnetic resonance spectroscopy used to identify the interactive binding surface of SecA
dimer
-
chemical cross-linking experiments, dimerization is necessary for the translocation ATPase activity of SecA, monomer-dimer equilibrium is altered in SecA mutants: mutants lacking 2 to 11 residues of the amino terminus of SecA failed to form dimers at 1microM SecA and 300 nM KCl, determination by gel filtration controlling eluate by photodiode array UV/Vis detector, a differential refractometer and a static, multiangle laser light scattering detector
dimer
subunit SecA1 forms homodimers with an apparent dimer dissociation constant of 65 nM at 30 mM KCl, microscale thermophoresis technique. No binding is observed at 300 mM KCl. Heterodimerization of subunit SecA1 and SecA2 is observed with an apparent Kd of 378 nM while the experiment in high salt buffer shows no interaction. SecA1/SecA2 heterodimers have a significantly lower affinity than the SecA1 or SecA2 homodimer
dimer
subunit SecA1 forms homodimers with an apparent dimer dissociation constant of Kd of 161 nM at 30 mM KCl, and a Kd of 618 nM at 150 mM KCl, microscale thermophoresis technique. No binding is observed at 300 mM KCl. Heterodimerization of subunit SecA1 and SecA2 is observed with an apparent Kd of 378 nM while the experiment in high salt buffer shows no interaction. SecA1/SecA2 heterodimers have a significantly lower affinity than the SecA1 or SecA2 homodimer
dimer
-
subunit SecA1 forms homodimers with an apparent dimer dissociation constant of Kd of 161 nM at 30 mM KCl, and a Kd of 618 nM at 150 mM KCl, microscale thermophoresis technique. No binding is observed at 300 mM KCl. Heterodimerization of subunit SecA1 and SecA2 is observed with an apparent Kd of 378 nM while the experiment in high salt buffer shows no interaction. SecA1/SecA2 heterodimers have a significantly lower affinity than the SecA1 or SecA2 homodimer
-
dimer
-
subunit SecA1 forms homodimers with an apparent dimer dissociation constant of 65 nM at 30 mM KCl, microscale thermophoresis technique. No binding is observed at 300 mM KCl. Heterodimerization of subunit SecA1 and SecA2 is observed with an apparent Kd of 378 nM while the experiment in high salt buffer shows no interaction. SecA1/SecA2 heterodimers have a significantly lower affinity than the SecA1 or SecA2 homodimer
-
dimer
-
TtSecA forms parallel (head-to-head) dimers that are reminiscent of open scissors. The dimer interface is abundant in bulky Arg and Lys side-chains from both subunits, which stack on one another to form a basic zipper that is highly conserved
homodimer
-
TAPL forms a homodimer in the membrane and under the solubilized conditions
homodimer
-
dissected in TMD0 (residues 1-142), containing a C-terminal myc-tag, and the core complex (residues 143-766), which consists of the cytosolic linker L0. Core-TAPL is essential and sufficient for peptide transport
homodimer
-
TAPL forms a homodimer in the membrane and under the solubilized conditions
monomer
X-ray diffraction reveals that the dimeric SecA ATPase dissociates in monomers during protein translocation
monomer
-
under most conditions, only the monomer form can be detected, indicating that dimers are very unstable. Monomers can interact at least transiently and are the important species during ATP hydrolysis
monomer
-
under most conditions, only the monomer form can be detected, indicating that dimers are very unstable. Monomers can interact at least transiently and are the important species during ATP hydrolysis
-
monomer
-
X-ray diffraction reveals that the dimeric SecA ATPase dissociates in monomers during protein translocation
additional information
-
SpaT, another ABC transporter encoded in the subtilin operon, role concluded from homologies to other ABC transporters
additional information
-
components involved are SpaF and SpaG, function concluded from similarities with ABC transporters belonging to the HisP subfamily where the ATP binding sites are located in the N-terminal part of the protein
additional information
-
SpaT, another ABC transporter encoded in the subtilin operon, role concluded from homologies to other ABC transporters
-
additional information
-
components involved are the membrane fusion protein PrtE, the outer membrane protein PrtF, and the ABC protein PrtD
additional information
-
components involved are two helper proteins and the ABC protein: membrane fusion protein (MFP), outer membrane protein (OMP), and the ABC protein
additional information
-
components involved are two helper proteins and the ABC protein: membrane fusion protein (MFP), outer membrane protein (OMP), and the ABC protein
additional information
the dimer, crosslinked by disulfide bridges, is inactive, the monomer is active
additional information
residues Leu6, the amino terminus (residues 2 to 11) in the nucleotide binding domain, Phe263 in the preprotein binding domain, and Tyr794 and Arg805 in the intramolecular regulator of the ATPase 1 domain are involved in ecSecA dimerization
additional information
Gram-negative bacteria
-
components involved are two helper proteins and the ABC protein: membrane fusion protein (MFP), outer membrane protein (OMP), and the ABC protein
additional information
Gram-negative bacteria
-
components involved are two helper proteins and the ABC protein: membrane fusion protein (MFP), outer membrane protein (OMP), and the ABC protein
additional information
-
components involved are encoded by lctF, lctE and lctG, role concluded from homologies to other ABC transporters
additional information
-
LcnC with one ATP binding domain in its C-terminus
additional information
-
LagD, role concluded from homologies to other ABC transporters
additional information
-
LagD, role concluded from homologies to other ABC transporters
-
additional information
-
ABC protein HasA and membrane fusion protein HasE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals diffracting to 2.4 A resolution are obtained using the vapour-diffusion technique with sitting drops. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 203.4, b = 49.8, c = 100.8 A, alpha = gamma = 90.0°, beta = 119°. A selenomethionine derivative is prepared
-
homology modeling based on the crystal structure of the Shewanella oneidensis peptide transporter PepTso, identifies Glu56 and Arg305 as potential periplasmic gating residues
molecular docking of inhibitor 2-((4-azidobenzyl)thio)-4-(4-(benzyloxy)phenyl)-6-oxo-1,6-dihydropyrimidine-5-carbonitrile. The azido group points towards hydrophilic residues including A/Asp512, A/Arg509, A/Gly510 and A/Thr511. The torsion around the -CH2O- atoms between the two phenyl groups allows the terminal phenyl group to rest in a pocket away from the hydrophilic residues B/Thr511, B/Gly510 and B/Glu487. Most of the active inhibitors seem to bind at the interface of chains A and B
EPR spectroscopy using covalently attached 2,2,5,5-tetramethylpyrrolidine-1-oxyl spin probes, and 2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid spin-labeled peptides. The side-chains' mobility is strongly restricted at the ends of the peptide, whereas the central region is flexible, suggesting a central peptide bulge. Peptides bind to TAP in an extended kinked structure, analogous to those bound to MHC class I proteins
-
extracellular domain from isoform PepT1, sitting drop vapor diffusion method, using 20% (w/v) polyethylene glycol 6000, 0.1 M MES (pH 6.0), and 0.2 M ammonium chloride
extracellular domain from isoform PepT2, sitting drop vapor diffusion method, using 0.2 M (NH4)3 citrate (pH 5.8) and 21% PEG (w/v) 3350
to 1.9 A resolution. Structure represents an intermediate state during the transition of the clamp from an open to a closed conformation. Closure of the clamp occurs in two phases, an initial movement of polypeptide cross-linking domain PPXD, helical scaffold domain HSD, and helical wing domain HWD as a unit, followed by a movement of PPXD alone toward nucleotide-binding domain NBD2. The substrate associates with the back of the clamp by dynamic hydrogen bonding and the clamp is laterally closed by a conserved loop of the PPXD
crystallization by hanging-drop vapour-diffusion technique in two different space groups P2(1(2))21 (a = b = 168.6 A, c = 149.8 A) and P6(1(5))22 (a = b = 130.9 A, c = 564.6 A). The crystals, improved by macroseeding, diffract to beyond 2.8 A and 3.5 A resolution for the trigonal and hexagonal crystal forms, respectively
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G55A
-
mutation in the potential ATP-binding site in ExeA, decreased rate of aerolysin secretion
G55D
-
mutation in the potential ATP-binding site in ExeA, decreased rate of aerolysin secretion
G55V
-
mutation in the potential ATP-binding site in ExeA, decreased rate of aerolysin secretion
K539M
-
introduction of a Walker A mutation in the haf-4 construct. The mutation in ATP-binding site of HAF-4 inhibits the maturation of granules as dominant-negative effects. The inactive form of HAF-4 does not rescue the phenotype
Cys-less
mutant for analyzing the interaction and regulatory domains of SecA
D209A
-
a dominant-negative mutant, binds ATP but is unable to hydrolyze it and is inactive in proOmpA translocation. Mutant generates a translocation intermediate of 18 kDa. Further addition of wild-type SecA causes its translocation into either mature OmpA or another intermediate of 28 kDa that can be translocated into mature by a proton motive force. The addition of excess D209N SecA during translocation causes a topology inversion of SecG
E20D
mutant is not affected by the bulk pH in the range tested, no dramatic change in IC50 value for peptides Gly-Lys, beta-Ala-Lys
E20Q
mutant is not affected by the bulk pH in the range tested, no dramatic change in IC50 value for peptides Gly-Lys, beta-Ala-Lys
E388D
increase in IC50 value for peptides Gly-Lys, beta-Ala-Lys, increase in pH-optimum
E388Q
increase in IC50 value for peptides Gly-Lys, beta-Ala-Lys, increase in pH-optimum
E400C
mutant for analyzing the interaction and regulatory domains of SecA
E400C/R642C
mutant for analyzing the interaction and regulatory domains of SecA
E400R
mutant for analyzing the interaction and regulatory domains of SecA
E400R/A628T
mutant for analyzing the interaction and regulatory domains of SecA
E400R/E619K
mutant for analyzing the interaction and regulatory domains of SecA
E400R/H620P
mutant for analyzing the interaction and regulatory domains of SecA
E400R/I627T
mutant for analyzing the interaction and regulatory domains of SecA
E400R/L610P
mutant for analyzing the interaction and regulatory domains of SecA
E400R/M607T
mutant for analyzing the interaction and regulatory domains of SecA
E400R/N629D
mutant for analyzing the interaction and regulatory domains of SecA
E635C
mutant for analyzing the interaction and regulatory domains of SecA
Ile3A
mutation completely blocks dimerization of SecA in 300 mM KCl buffer
K108R
mutant, defective in ATP binding and protein translocation in vitro, as well as biologically inactive in vivo
Leu2A
mutation completely blocks dimerization of SecA in 300 mM KCl buffer
Leu5A
mutation completely blocks dimerization of SecA in 300 mM KCl buffer
Leu6A
mutation completely blocks dimerization of SecA in 300 mM KCl buffer
N95
truncated version of Escherichia coli SecA, the last 70 residues are lacking
N95CC
two cysteines are introduced into a truncated version of Escherichia coli SecA, at position 636 and 801, the last 70 residues are lacking, mutant is dimeric and fully functional
Phe10A
mutation completely blocks dimerization of SecA in 300 mM KCl buffer
R400R/M607T
mutant for analyzing the interaction and regulatory domains of SecA
R642C
mutant for analyzing the interaction and regulatory domains of SecA
R642E
mutant for analyzing the interaction and regulatory domains of SecA
R642E/A628T
mutant for analyzing the interaction and regulatory domains of SecA
R642E/E619K
mutant for analyzing the interaction and regulatory domains of SecA
R642E/H620P
mutant for analyzing the interaction and regulatory domains of SecA
R642E/I627T
mutant for analyzing the interaction and regulatory domains of SecA
R642E/L610P
mutant for analyzing the interaction and regulatory domains of SecA
R642E/M607T
mutant for analyzing the interaction and regulatory domains of SecA
R642E/N629D
mutant for analyzing the interaction and regulatory domains of SecA
R656C
mutant for analyzing the interaction and regulatory domains of SecA
SecADELTA11/N95
monomeric SecA derivative mutant, which lacks extreme terminal residues and shows in vitro and in vivo activities
V9A/F10A
mutation enhances dissociation by 8fold with respect to that of wild-type SecA
Val9A
mutation completely blocks dimerization of SecA in 300 mM KCl buffer
Y477W
-
KM-value for ATP is 1.75fold higher than wild-type value. kcat for ATP is 4.3fold higher than wild-type value
K115A
mutant, substitution of the conserved lysine in the Walker A motif eliminates ATP binding and affects the biological activity
K115R
mutant, substitution of the conserved lysine in the Walker A motif eliminates ATP binding and affects the biological activity
K115A
-
mutant, substitution of the conserved lysine in the Walker A motif eliminates ATP binding and affects the biological activity
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K115R
-
mutant, substitution of the conserved lysine in the Walker A motif eliminates ATP binding and affects the biological activity
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SecA2DELTA1-990
mutant, cloned into different plamids, construction of different strains
SecA2DELTA1732-2397 7
mutant, cloned into different plamids, construction of different strains
SecA2DELTA1768-2028
mutant, cloned into different plamids, construction of different strains
SecA2DELTA991-1749
mutant, cloned into different plamids, construction of different strains
E485R/E488R/R367E
mutation leads to a closed conformation of the clamp, the C-loop remains inside the clamp
R367E
mutation of a conserved residue, results in significant lateral opening of the clamp, which leads to increased dissociation of the substrate
E485R/E488R/R367E
-
mutation leads to a closed conformation of the clamp, the C-loop remains inside the clamp
-
R367E
-
mutation of a conserved residue, results in significant lateral opening of the clamp, which leads to increased dissociation of the substrate
-
additional information
additional information
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large in-frame deletion of SpaT, not translocation is interrupted, but proteolytic cleavage of the leader segment while the precurser resides in the cell wall
additional information
-
large in-frame deletion of SpaT, not translocation is interrupted, but proteolytic cleavage of the leader segment while the precurser resides in the cell wall
-
additional information
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the loss-of-function mutants for haf-4 and haf-9, constructed by RNAi mechanism, exhibit granular defects in late larval and young adult intestinal cells, associated with decreased brood size, prolonged defecation cycle, and slow growth. The intestinal granular phenotype is rescued by the overexpression of the GFP-tagged wild-type protein, but not by the ATP-unbound form of HAF-4, overview
additional information
deletion of SecA1 failed, unless a copy of the gene is provided in trans on a plasmid, thus SecA1 belongs to the housekeeping genes
additional information
deletion of SecA1 failed, unless a copy of the gene is provided in trans on a plasmid, thus SecA1 belongs to the housekeeping genes
additional information
deletion of SecA2 failed, unless a copy of the gene is provided in trans on a plasmid, thus SecA2 belongs to the housekeeping genes
additional information
deletion of SecA2 failed, unless a copy of the gene is provided in trans on a plasmid, thus SecA2 belongs to the housekeeping genes
additional information
a collection of 63 monocysteine mutants for the 901-aminoacid-residue SecA protein is generated for topological analysis of the protein
additional information
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a collection of 63 monocysteine mutants for the 901-aminoacid-residue SecA protein is generated for topological analysis of the protein
additional information
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SecY-SecA interactions are studied by an in vivo site-directed cross-linking technique
additional information
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analysis of the function of the two-helix finger of the SecA ATPase via point mutations
additional information
screening of a library of mutants to identify amino acids critical for peptide transport and identification of 35 single point mutations that result in a full or partial loss of transport activity
additional information
-
screening of a library of mutants to identify amino acids critical for peptide transport and identification of 35 single point mutations that result in a full or partial loss of transport activity
additional information
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construction of SecA N-terminal deletion mutants. The first small helix, the linker and part of the second helix (residues 2-22) are dispensable for SecA activity in complementing the growth of a SecA temperature-sensitive mutant. Deletions of N-terminal aminoacyl residues 23-25 result in severe progressive retardation of growth. A decrease of SecA activity caused by N-terminal deletions correlates to the loss of SecA membrane binding, formation of lipid-specific domains and channel activity. The N-terminal aminoacyl residues 23-25 play a critical role for SecA binding to membranes and the N-terminal limit of SecA for activity is at the 25th amino acid
additional information
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mutant pairs of TAP1/TAP2 with mutation in ABC signature motif, C-loop. Chimera with two canonical C-loops show highest transport activity, chimera with two degenerate C-loops have lowest transport rates. All single mutants and chimera show similar activities in peptide or ATP binding
additional information
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knockdown of the ABC transporter enzyme in WM793B cells by shRNA leads to increases the sensitivity of cells to doxorubicin and reduces the cell survival, overview
additional information
analysis of the function of SecA1 and SecA2 via several mutants
additional information
analysis of the function of SecA1 and SecA2 via several mutants
additional information
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analysis of the function of SecA1 and SecA2 via several mutants
additional information
analysis of the function of SecA1 and SecA2 via several mutants
additional information
analysis of the function of SecA1 and SecA2 via several mutants
additional information
-
analysis of the function of SecA1 and SecA2 via several mutants
additional information
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isoform PTR6 is able to complement transport defects in a yeast ptr2 mutant strain
additional information
analysis of the function of SecA via mutants and SecA-SecA2-chimeras
additional information
analysis of the function of SecA via mutants and SecA-SecA2-chimeras
additional information
-
analysis of the function of SecA via mutants and SecA-SecA2-chimeras
additional information
analysis of the function of SecA2 via mutants and SecA-SecA2-chimeras
additional information
analysis of the function of SecA2 via mutants and SecA-SecA2-chimeras
additional information
-
analysis of the function of SecA2 via mutants and SecA-SecA2-chimeras
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
SecYEG binding stabilizes a cold sodium dodecylsulfate-resistant dimeric state of SecA
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, the ATPase domain is indefinitly stable in phosphate or Tris buffer, pH 8, in the absence of ATP concentrations of up to 25 mg/ml
-
4°C, the ATPase domain is stable for at least 2 days in phosphate or Tris buffer, pH 8, in the absence of ATP concentrations of up to 25 mg/ml
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crude membranes containing TAPL are prepared from Sf9 insect cells, furthermore a SP Sepharose Fast Low column and a Zn2+-iminodiacetate column are used
-
inverted membrane vesicles are prepared
recombinant TAPL from membranes of Drosophila melanogaster S2 cells by detergent solubilization, and ADP or ATP affinity chromatography, not by AMP affinity
using a Q-Sepharose 26/10 anion-exchange column, a SP-Sepharose 16/5 cation exchange column, and a Superose 12 HR gel filtration column
using osmotic shock, a SP-Sepharose 26/10 packed cation-exchange column, and a Sephacryl-200 HR 16/90 packed column
recombinant TAPL from membranes of Drosophila melanogaster S2 cells by detergent solubilization, and ADP or ATP affinity chromatography, not by AMP affinity
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recombinant TAPL from membranes of Drosophila melanogaster S2 cells by detergent solubilization, and ADP or ATP affinity chromatography, not by AMP affinity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a set of N-terminally truncated human TAP variants are generated, PCR products are cloned into the vector pFASTBac Dual for expression in the Baculovirus system
-
baculoviruses encoding a histidine-tagged and a green fluorescent protein tagged version of TAP1, and a yellow fluorescent protein-tagged version of TAP2 are obtained
-
expressed in Escherichia coli after stimulation with 1 mM isopropyl-beta-D-thiogalactoside
-
expressed in Escherichia coli strain BL21(DE3) harboring a special plasmid
expressed in Escherichia coli strain Bl21DE3 as a recombinant C-terminal His6-tagged protein
expression of a truncated form of SecA lacking the C-terminal inhibitory domain
genes haf-4 and haf-5, phylogenetic tree, overexpression of wild-type and mutant GFP-tagged enzymes
-
human TAPL is cloned into pEGFP-N3 and pIRES2-EGFP resulting in TAPL with a C-terminal EGFP and TAPL co-translated EGFP, respectively, TAPL containing a C-terminal myc-tag is cloned into pcDNA3.1+, and into the retroviral vector pLPCX
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into the pET-27b+ vector for expression in Escherichia coli BL21DE3 cells
into the pET29a vector for expression in Escherichia coli BL21DE3 cells
into the pET41b vector for expression in Escherichia coli BL21DE3 cells
into the pET5a vector for expression in Escherichia coli BL21DE3 cells
isozyme 12A, expression of TAPL in membranes of Drosophila melanogaster S2 cells
plasmid pT7secA-Cys-0, a derivative of pT7secA2 that has all four cysteine codons within secA changed to serine, is used to create the monocysteine secA mutants
recombinant baculovirus, encoding human TAP1 and TAP2, is used for infection of Sf9 cells, used for the peptide transport assay
-
TAPL containing a C-terminal His10 tag or a Strep-tag II is cloned for expression in Sf9 insect cells infected with recombinant baculovirus
-
the coding sequence of the nucleotide-binding domain of TAP1, amino acids 489-748, is cloned into the pET21a+ vector
-
the DNA fragment encoding the N-terminal 236 amino acid residues is cloned into the pET20b vector for expression in Escherichia coli BL21.19 cells
the secA2 gene of Mycobacterium smegmatis is cloned from pMB208 into pMV306.kan to generate pYA810
expressed in Escherichia coli strain Bl21DE3 as a recombinant C-terminal His6-tagged protein
-
expressed in Escherichia coli strain Bl21DE3 as a recombinant C-terminal His6-tagged protein
isozyme 12A, expression of TAPL in membranes of Drosophila melanogaster S2 cells
-
isozyme 12A, expression of TAPL in membranes of Drosophila melanogaster S2 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
peptide transporter 1 mRNA expressions is increased at 5-7 days post hatching
short-term fasting results in up-regulation of PepT1 mRNA levels, while prolonged fasting results in down-regulation. The resumption of feeding results in up-regulation of PepT1 above pre-fasted levels
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
SecA2-His6 protein is purified from inclusion bodies and refolded
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EXTERNAL LINKS (specific for EC-Number 7.4.2.5)
Transporter Classification Database (TCDB): 3.A.1.109.8
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Release 2023.1 (January 2023)
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