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Information on EC 7.3.2.7 - arsenite-transporting ATPase
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7.3.2.7 arsenite-transporting ATPaseIUBMB Comments
This bacterial transporter does not belong to the ABC superfamily, and instead is a member of its own family, referred to as the Ars family. The enzyme usually contains two subunits where one (with 12 membrane-spanning segments) forms the 'channel' part and the other (occurring in pairs peripherally to the membrane) contains the ATP-binding site. It forms an arsenite efflux pump that removes arsenite from the cytoplasm, and can also remove antimonite anions.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
asna1, arsa atpase, asna-1, arsab, arsab pump, giarsa, riarsb, arsenite-translocating atpase, arsab extrusion pump, arsab as(iii) efflux pump, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACR3
ACR3-ArsC
ACR3-ArsC fusion protein
ARSA
ArsA ATPase
ArsAB
ArsAB pump
Arsenical resistance ATPase
-
-
-
-
Arsenite-translocating ATPase
Arsenite-transporting ATPase
-
-
-
-
ATP-dependent arsenite pump
-
-
-
-
EC 3.6.3.16
-
-
formerly
-
RiArsB
-
arsenate/arsenite permease component of ArsAB arsenite efflux pump
Rv2643
ARSA
-
-
-
-
ArsA ATPase
-
-
Arsenite-translocating ATPase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + arsenite[side 1] = ADP + phosphate + arsenite[side 2]
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (arsenite-exporting)
This bacterial transporter does not belong to the ABC superfamily, and instead is a member of its own family, referred to as the Ars family. The enzyme usually contains two subunits where one (with 12 membrane-spanning segments) forms the 'channel' part and the other (occurring in pairs peripherally to the membrane) contains the ATP-binding site. It forms an arsenite efflux pump that removes arsenite from the cytoplasm, and can also remove antimonite anions.
CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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 + arsenate/in
ADP + phosphate + arsenate/out
-
in absence of the ArsC protein, MW 16000 Da, the the pump only transports arsenite and antimonite. The ArsC protein alters the specificity of the pump to allow recognition and transport of arsenate
-
?
ATP + H2O + antimonite/in
ADP + phosphate + antimonite/out
-
-
-
-
?
ATP + H2O + antimonite/in
ADP + phosphate + antimonite/out
-
-
-
-
?
ATP + H2O + antimonite/in
ADP + phosphate + antimonite/out
-
the arsenic chaperone ArsD transfers trivalent metalloids to ArsA, the catalytic subunit of an As(III)-Sb(III) efflux pump. Interaction with ArsD increases the affinity of ArsA for antimonite, thus increasing its ATPase activity at lower concentrations of antimonite, regulatory mechanism, overview
-
-
?
ATP + H2O + antimonite/in
ADP + phosphate + antimonite/out
-
-
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
-
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
ASNA-1 , encoding a functional ArsA ATPase, is critical for As(III) and Sb(III) tolerance in the intact organism, the enzyme does not provide resistance to other metals, e.g. Cu2+ or Pb2+, overview
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
-
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
the ars operon confers resistance to arsenite, arsenate and antimonite
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
the ars genes are transcribed in the presence of an inducer, arsenite. Segmental differences in stability within the polycistronic transcript are proposed to account for the differential expression of the ars genes
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
mechanism of transcriptional regulation by the ArssR repressor and allosteric regulation of the ArsA protein, the catalytic subunit of the pump
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
detoxifying system
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
ArsA ATPase is the catalytic subunit of the ArsAB pump, ArsD is an arsenic chaperone to the ArsAB pump, transferring the trivalent metalloids As(III) and Sb(III) to the ArsA subunit of the pump thereby increasing the affinity of ArsA for As(III), resulting in increased rates if extrusion and resistance to environmentally relevant concentrations of arsenite
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
ArsD residues Cys12, Cys13, and Cys18, but not Cys112, Cys113, Cys119, or Cys120, from an As(III)-binding site are required for arsenic metallochaperone activity, ArsD is a metallochaperone that delivers As(III) to ArsA, increasing its affinity for As(III), thus conferring resistance to environmental concentrations of arsenic, ArsD mutants with alanines substituting for Cys112, Cys113, Cys119, or Cys120 individually or in pairs or truncations lacking the vicinal pairs retain the ability to interact with ArsA and to activate its ATPase activity, mutational interaction analysis, overview
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
the ArsAB extrusion pump confers resistance to the toxic trivalent metalloids arsenite [As(III)] and antimonite [Sb(III)], overview
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
the arsenic chaperone ArsD transfers trivalent metalloids to ArsA, the catalytic subunit of an As(III)-Sb(III) efflux pump. Interaction with ArsD increases the affinity of ArsA for arsenite, thus increasing its ATPase activity at lower concentrations of arsenite and enhancing the rate of arsenite extrusion rendering cells resistant to environmental concentrations of arsenic, regulatory mechanism, overview
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
ArsA ATPase is the catalytic subunit of the ArsAB pump
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
ArsA ATPase, the catalytic subunit of the pump, has two homologous halves, A1 and A2, and at the interface of these two halves are two nucleotide-binding domains and a metalloid-binding domain, Cys113 and Cys422 form a high-affinity metalloid binding site. Two other metalloid atoms are bound, one liganded to Cys172 and His453, and the other liganded to His148 and Ser420, but there is only a single high-affinity metalloid binding site in ArsA, and second that Cys172 controls the affinity of this site for metalloid and hence the efficiency of metalloactivation of the ArsAB efflux pump, metalloid binding site MBS structure and mechanism, overview
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
metalloid-binding site MBS1 is involved in metalloid transfer and ArsA activation
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
Asp142 is involved in Mg2+ binding and also plays a role in signal transduction between the catalytic and activation domains. In contrast, Asp447 is not nearly as critical for Mg2+ binding as Asp142 but appears to be in communication between the metal and catalytic sites
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
binding of As(III) to ArsA is greatly facilitated by the presence of magnesium ion and ATP
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
ArsA has a high-affinity metalloid binding site composed of Cys113 and Cys422, and a third residue, Cys172, that participates in high-affinity binding and activation of ATP hydrolysis
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
the enzyme is composed of ATPase subunit ArsA and arsenic-efflux pump ArsB. ArsA/ArsB ATPase efflux/influx pump in membrane associated uptake, efflux/influx, oxidation and reduction of arsenic ion, overview
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
the ars operon confers resistance to arsenite, arsenate and antimonite
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
the ars operon confers resistance to arsenite, arsenate and antimonite
-
-
?
ATP + H2O + arsenite[side 1]
ADP + phosphate + arsenite[side 2]
-
-
-
-
?
additional information
?
-
-
the AmArsA1-AmArsA2 complex has metalloid-stimulated ATPase activity. ArsB transports antimonite, while Acr3 does not appear to do so
-
-
?
additional information
?
-
-
the ArsA protein is a membrane associated ATPase, energizing the arsenite efflux pump by ATP hydrolysis, ArsA is attached to the ArsB inner-membrane protein. The ArsB protein can function alone as a chemiosmotic, membrane-potential driven arsenite-efflux transporter or together with ArsA as an ATP-driven primary membrane pump. ArsC converts the less toxic arsenate to more toxic arsenite, the substrate for the ArsB transport protein
-
-
?
additional information
?
-
-
The ArsA protein exhibits ATPase activity with a strict requirement for arsenite or antimonite. The binding of the ArsA protein to the ArsB protein on the inner membrane forms an active pump complex which catalyzes oxyanion transport, ArsB functions as the membrane anchor for the ArsA protein
-
-
?
additional information
?
-
-
Trp141 moves into a relatively more polar environment upon binding of MgADP- and is a sensitive probe for the binding of the product of hydrolysis. The conserved domain of the ArsA subunit is an energy transduction domain that might be involved in the transmission of energy of ATP hydrolysis to other functions such as transport of arsenite through the ArsB subunit of the oxyanion pump
-
-
?
additional information
?
-
-
ArsA specifically interacts with ArsD but not with ArsR or ArsC
-
-
?
additional information
?
-
the mutant chimeric NifH-ArsA2 can substitute for the ArsA in arsenic reduction, overview
-
-
?
additional information
?
-
-
ArsA exhibits a low, basal rate of ATPase activity in the absence of As(III) or Sb(III) and a higher, activated rate in their presence
-
-
?
additional information
?
-
-
ArsA is the catalytic subunit of the ArsAB arsenite (As(III)) translocating ATPase, ArsA exhibits ATpase activity
-
-
?
additional information
?
-
-
Lys16 is not critical for ATPase activity, while Lys335 is involved in intersubunit interaction and activation of ATPase activity in both halves of the protein
-
-
?
additional information
?
-
-
Lys16 is not critical for ATPase activity, while Lys335 is involved in intersubunit interaction and activation of ATPase activity in both halves of the protein
-
-
?
additional information
?
-
ASNA1, an ATPase targeting tail-anchored proteins, regulates melanoma cell growth and sensitivity to cisplatin and arsenite. ASNA1 is also an essential ATPase for the insertion of tail-anchored proteins into endoplasmic reticulum membranes and a regulator of insulin secretion. ASNA1 expression is necessary for growth.
-
-
?
additional information
?
-
-
ASNA1, an ATPase targeting tail-anchored proteins, regulates melanoma cell growth and sensitivity to cisplatin and arsenite. ASNA1 is also an essential ATPase for the insertion of tail-anchored proteins into endoplasmic reticulum membranes and a regulator of insulin secretion. ASNA1 expression is necessary for growth.
-
-
?
additional information
?
-
ATP-binding cassette transports, binding affinities and associating ratable constants show that As-binding is comparatively insensitive to the location of the residues within the moderately stable alpha-helical structure in ArsB, overview
-
-
?
additional information
?
-
ATP-binding cassette transports, binding affinities and associating ratable constants show that As-binding is comparatively insensitive to the location of the residues within the moderately stable alpha-helical structure in ArsB, overview
-
-
?
additional information
?
-
ATP-binding cassette transports, binding affinities and associating ratable constants show that As-binding is comparatively insensitive to the location of the residues within the moderately stable alpha-helical structure in ArsB, overview
-
-
?
additional information
?
-
-
ATP-binding cassette transports, binding affinities and associating ratable constants show that As-binding is comparatively insensitive to the location of the residues within the moderately stable alpha-helical structure in ArsB, overview
-
-
?
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 + antimonite/in
ADP + phosphate + antimonite/out
-
-
-
-
?
ATP + H2O + antimonite/in
ADP + phosphate + antimonite/out
-
-
-
-
?
ATP + H2O + antimonite/in
ADP + phosphate + antimonite/out
-
the arsenic chaperone ArsD transfers trivalent metalloids to ArsA, the catalytic subunit of an As(III)-Sb(III) efflux pump. Interaction with ArsD increases the affinity of ArsA for antimonite, thus increasing its ATPase activity at lower concentrations of antimonite, regulatory mechanism, overview
-
-
?
ATP + H2O + antimonite/in
ADP + phosphate + antimonite/out
-
-
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
-
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
ASNA-1 , encoding a functional ArsA ATPase, is critical for As(III) and Sb(III) tolerance in the intact organism, the enzyme does not provide resistance to other metals, e.g. Cu2+ or Pb2+, overview
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
-
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
the ars operon confers resistance to arsenite, arsenate and antimonite
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
the ars genes are transcribed in the presence of an inducer, arsenite. Segmental differences in stability within the polycistronic transcript are proposed to account for the differential expression of the ars genes
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
mechanism of transcriptional regulation by the ArssR repressor and allosteric regulation of the ArsA protein, the catalytic subunit of the pump
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
detoxifying system
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
ArsA ATPase is the catalytic subunit of the ArsAB pump, ArsD is an arsenic chaperone to the ArsAB pump, transferring the trivalent metalloids As(III) and Sb(III) to the ArsA subunit of the pump thereby increasing the affinity of ArsA for As(III), resulting in increased rates if extrusion and resistance to environmentally relevant concentrations of arsenite
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
ArsD residues Cys12, Cys13, and Cys18, but not Cys112, Cys113, Cys119, or Cys120, from an As(III)-binding site are required for arsenic metallochaperone activity, ArsD is a metallochaperone that delivers As(III) to ArsA, increasing its affinity for As(III), thus conferring resistance to environmental concentrations of arsenic, ArsD mutants with alanines substituting for Cys112, Cys113, Cys119, or Cys120 individually or in pairs or truncations lacking the vicinal pairs retain the ability to interact with ArsA and to activate its ATPase activity, mutational interaction analysis, overview
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
the ArsAB extrusion pump confers resistance to the toxic trivalent metalloids arsenite [As(III)] and antimonite [Sb(III)], overview
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
the arsenic chaperone ArsD transfers trivalent metalloids to ArsA, the catalytic subunit of an As(III)-Sb(III) efflux pump. Interaction with ArsD increases the affinity of ArsA for arsenite, thus increasing its ATPase activity at lower concentrations of arsenite and enhancing the rate of arsenite extrusion rendering cells resistant to environmental concentrations of arsenic, regulatory mechanism, overview
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
binding of As(III) to ArsA is greatly facilitated by the presence of magnesium ion and ATP
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
the enzyme is composed of ATPase subunit ArsA and arsenic-efflux pump ArsB. ArsA/ArsB ATPase efflux/influx pump in membrane associated uptake, efflux/influx, oxidation and reduction of arsenic ion, overview
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
the ars operon confers resistance to arsenite, arsenate and antimonite
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
the ars operon confers resistance to arsenite, arsenate and antimonite
-
-
?
ATP + H2O + arsenite[side 1]
ADP + phosphate + arsenite[side 2]
-
-
-
-
?
additional information
?
-
ASNA1, an ATPase targeting tail-anchored proteins, regulates melanoma cell growth and sensitivity to cisplatin and arsenite. ASNA1 is also an essential ATPase for the insertion of tail-anchored proteins into endoplasmic reticulum membranes and a regulator of insulin secretion. ASNA1 expression is necessary for growth.
-
-
?
additional information
?
-
-
ASNA1, an ATPase targeting tail-anchored proteins, regulates melanoma cell growth and sensitivity to cisplatin and arsenite. ASNA1 is also an essential ATPase for the insertion of tail-anchored proteins into endoplasmic reticulum membranes and a regulator of insulin secretion. ASNA1 expression is necessary for growth.
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
As3+
Mg2+
Sb3+
As3+
activates the ATPase activity of the ASNA-1 protein 2.0fold, Km is 3.54 mM at ATP saturation
Sb3+
activates the ATPase activity of the ASNA-1 protein 4.6fold, Km is 0.04 mM at ATP saturation
Sb3+
-
ArsA is activated by binding of Sb(III), and both wild-type and mutant K16Q ArsAs bind Sb(III) with a 1:1 stoichiometry
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diethyl dicarbonate
-
inhibition could be reversed upon subsequent incubation with hydroxylamine
Trypsin
-
trypsin cleaves the ArsA at Arg290 to produce a 32 kDa A1 fragment that is catalytically inactive and remains stable to trypsin digestion, and a slightly smaller A2 fragment which is digested rapidly. The trypsin digestion pattern is much different when all three ligands, ATP, Sb(III), and Mg2+, are added together, conditions that produce activated catalysis, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
in vivo, cytosolic As(III) is nearly completely complexed with GSH. GSH greatly increases the rate of binding of As(III) to ArsD, but GSH does not affect the As(III)-stimulated ArsA ATPase activity
-
antimonite
-
activates 10fold the ATPase activity of wild-type ArsA, activation rates of mutants, overview
ArsD
-
ArsD is an arsenic metallochaperone that delivers As(III) to the ArsA ATPase of the ArsAB pump, transferring the trivalent metalloids As(III) and Sb(III) to the ArsA subunit of the pump thereby increasing the affinity of ArsA for As(III), resulting in increased rates if extrusion and resistance to environmentally relevant concentrations of arsenite, mutational analysis of metalloid binding sites involved in As(III) transport and resistance, overview
-
ArsD
-
encoded in the arsRDABC operon, the dimeric arsenic chaperone ArsD transfers trivalent metalloids to ArsA, the catalytic subunit of an As(III)-Sb(III) efflux pump. Interaction with ArsD increases the affinity of ArsA for arsenite and antimonite , thus increasing its ATPase activity at lower concentrations of arsenite 60fold, as well as for antimonite, and enhancing the rate of arsenite extrusion rendering cells resistant to environmental concentrations of arsenic, overview, cannot be replaced by DTT
-
ArsD
-
a metallochaperone that delivers trivalent metalloids [As(III) or Sb(III)] to the ArsA ATPase, the catalytic subunit of the ArsAB pump. ArsD residues Cys12, Cys13, and Cys18 are involved in the transfer of As(III) to ArsA
-
ArsD
-
ArsD is a metallochaperone which sequesters arsenite and antimonite and transfers them to the ArsA ATPase increasing the apparent affinity of ArsA for its substrates and lowering the concentration of free As(III) and Sb(III) in the cytosol
-
ArsD
-
ArsD is an arsenic chaperone for ArsA. ArsD transfers As(III) to ArsA and increases the affinity of ArsA for As(III). Cys12, Cys13 and Cys18 in ArsD form a three sulfur-coordinated As(III) binding site that is essential for metallochaperone activity, Interaction between ArsD and ArsA, ArsD function, overview
-
ArsD
-
arsenic metallochaperone ArsD delivers As(III) to the ArsA ATPase, the catalytic subunit of the ArsAB pump. ArsD binds one arsenic per monomer coordinated with the three sulfur atoms of Cys12, Cys13 and Cys18, modeling of ArsD with and without bound As(III), overview. For analysis of metallo chaperone activity a recombinant truncated form, ArsD109, is used
-
arsenite
-
activates 3fold the ATPase activity of wild-type ArsA, activation rates of mutants, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
activation kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
kinetics study of ArsA-As(III) binding
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28.87
purified recombinant MBP-fusion enzyme stimulated by 0.5 mM Sb3+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
transfer of As(III) from ArsD to ArsA occurs in the presence of MgATP at 23°C but not at 4°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two ars operons, ars1 and ars2, the arsA gene is split in halves, amarsA1 and amarsA2, and, acr3 but not an arsB gene coexists with arsA
-
-
-
-
-
gene arsA, encoding for the catalytic subunit of the the ArsAB pump
Uniprot
gene arsAB in the arsRDABC operon is encoded on intracellular plasmid R773
-
-
strains JM109 and BL21, ArsA ATPase is the catalytic subunit of the ArsAB pump encoded by the arsRDABC operon of Escherichia coli plasmid R773
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
ArsA protein is an extrinsic membrane protein, ArsB protein is an integral membrane protein
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
-
phylogenetic analysis of gene arsA and prokaryotic and eukaryotic ArsA homologues with detailed analysis of clustering in the superfamily, overview
evolution
-
the ArsA ATPase belongs to the P-loop GTPase subgroup within the GTPase superfamily of proteins, members of this subgroup have a deviant Walker A motif
evolution
-
the ArsA ATPase belongs to the P-loop GTPase subgroup within the GTPase superfamily of proteins, members of this subgroup have a deviant Walker A motif
-
malfunction
-
mutations rendered the aquaglyceroporin channel more polar resulting in lower glycerol permeability and enhanced arsenite selectivity
malfunction
-
while Lys16 mutants show similar resistance phenotypes as the wild type, the Lys335 mutants are sensitive to higher concentrations of arsenite. The As(III)/Sb(III) binding affinity decreases in the order ArsA wild-type > K16Q > K335Q
malfunction
-
while Lys16 mutants show similar resistance phenotypes as the wild type, the Lys335 mutants are sensitive to higher concentrations of arsenite. The As(III)/Sb(III) binding affinity decreases in the order ArsA wild-type > K16Q > K335Q
-
physiological function
-
AmArsA1-AmArsA2 interaction is needed to form the functional ArsA ATPase. This novel AmArsA1-AmArsA2 complex may provide insight in how it participates with Acr3 in arsenite detoxification. ArsB transports antimonite, while Acr3 does not appear to do so
physiological function
-
ArsA is an ATPase that is the catalytic subunit of the ArsAB As(III) extrusion pump, and ArsD is an arsenic chaperone for ArsA. ArsD transfers As(III) to ArsA and increases the affinity of ArsA for As(III), allowing resistance to environmental concentrations of arsenic. ATP hydrolysis by ArsA is required for transfer of As(III) from ArsD to ArsA, suggesting that transfer occurs with a conformation of ArsA that transiently forms during the catalytic cycle. Docking of ArsD with ArsA, modeling and mechanism, detailed overview. Cysteine-rich metalloid binding sites of ArsD and ArsA come close to each other during interaction, ArsD interacts with nucleotide-bound form. The interface with ArsA involves one surface of alpha1 helix and metalloid binding site of ArsD. ArsB is a As(OH)3/H+ antiporter that extrudes As(III), conferring resistance
physiological function
-
subunit ArsA exhibuts ATPase activity and subunit ArsB is a 12 alpha-helix transmembrane spanning pump extruding As(III) and Sb(III). Transport via ArsB can be energized by the pmf or by forming an oxyanion translocating complex with the catalytic ArsA subunit, coupling ATP hydrolysis to efflux
physiological function
-
the actinomycete from marine environment harbors a fusion protein consisting of an aquaglyceroporin-derived arsenite channel with a C-terminal arsenate reductase domain of phosphotyrosine-phosphatase origin, providing transposable, single gene-encoded arsenate resistance. The arsenate reductase domain couples to thioredoxin and can complement arsenate-sensitive yeast strains. A second isoform Strop1447 with a nonfunctional channel is coupled to the mycothiol/mycoredoxin system and may use the mycothiol/mycoredoxin cofactor pool. The channel-enzyme fusion protein, Strop634, confers arsenate resistance in Salinispora tropica
physiological function
-
the arctinobacterium from soil harbors a fusion protein consisting of an aquaglyceroporin-derived arsenite channel with a C-terminal arsenate reductase domain of phosphotyrosine-phosphatase origin, providing transposable, single gene-encoded arsenate resistance
physiological function
-
the ArsAB pump in Escherichia coli, encoded by the ars operon of plasmid R773, confers resistance to arsenicals and antimonials. ArsA is the catalytic subunit of the pump that hydrolyzesATP in the presence of arsenite [As(III)] or antimonite [Sb(III)]. ATP hydrolysis is coupled to extrusion of As(III) or Sb(III) through ArsB, which serves both as a membrane anchor for ArsA and as the substrate-conducting pathway
physiological function
-
the bacterium harbors a fusion protein consisting of an aquaglyceroporin-derived arsenite channel with a C-terminal arsenate reductase domain of phosphotyrosine-phosphatase origin, providing transposable, single gene-encoded arsenate resistance. Strop634 and the ACR3-ArsC fusion protein Rv2643 from Mycobacterium tuberculosis are able to detoxify arsenate, whereas Strop1447 and two chimeras with Strop634 carrying either the Strop1447 channel or ArsC domain are not
physiological function
-
the catalytic subunit of the ArsAB arsenite (As(III)) translocating ATPase, is one of the five proteins encoded by the arsenical resistance (ars) operon of plasmid R773 in cells of Escherichia coli, that confers resistance to trivalent and pentavalent salts of the metalloid arsenic
physiological function
-
the ArsAB pump in Escherichia coli, encoded by the ars operon of plasmid R773, confers resistance to arsenicals and antimonials. ArsA is the catalytic subunit of the pump that hydrolyzesATP in the presence of arsenite [As(III)] or antimonite [Sb(III)]. ATP hydrolysis is coupled to extrusion of As(III) or Sb(III) through ArsB, which serves both as a membrane anchor for ArsA and as the substrate-conducting pathway
-
physiological function
-
the bacterium harbors a fusion protein consisting of an aquaglyceroporin-derived arsenite channel with a C-terminal arsenate reductase domain of phosphotyrosine-phosphatase origin, providing transposable, single gene-encoded arsenate resistance. Strop634 and the ACR3-ArsC fusion protein Rv2643 from Mycobacterium tuberculosis are able to detoxify arsenate, whereas Strop1447 and two chimeras with Strop634 carrying either the Strop1447 channel or ArsC domain are not
-
additional information
-
ARsA ATPase contains a deviant Walker A motif which has a signature lysine that is predicted to make intermonomer contact with the bound nucleotides and to play a role in ATP hydrolysis. ArsA has two signature lysines located at positions 16 and 335. Both wild-type and K16Q adopt a similar conformation during activated catalysis, whereas K335Q adopts a conformation that is resistant to trypsin cleavage
additional information
-
ArsD is a metallochaperone that delivers trivalent metalloids [As(III) or Sb(III)] to the ArsA ATPase, the catalytic subunit of the ArsAB pump. ArsD residues Cys12, Cys13, and Cys18 are involved in the transfer of As(III) to ArsA. Transfer of As(III) from ArsD to ArsA occurs in the presence of MgATP, neither MgADP nor MgATP-gamma-S can replace MgATP. Transfer occurs with a conformation of ArsA that transiently forms during the catalytic cycle and not simply to the closed conformation that ArsA adopts when As(III) and MgATP are bound
additional information
-
for arsenite transport, metallated ArsD interacts with and transfers As(III) to ArsA during catalysis, when the ATPase cycles between open to closed conformations, structure and ArsD-ArsA interaction analysis, docking of ArsD and ArsA and modeling, overview
additional information
-
the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain
additional information
-
the Strop634 channel domain has enhanced selectivity for arsenite and low glycerol permeability
additional information
-
ARsA ATPase contains a deviant Walker A motif which has a signature lysine that is predicted to make intermonomer contact with the bound nucleotides and to play a role in ATP hydrolysis. ArsA has two signature lysines located at positions 16 and 335. Both wild-type and K16Q adopt a similar conformation during activated catalysis, whereas K335Q adopts a conformation that is resistant to trypsin cleavage
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ARSA_ACIMA
Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / NBRC 100883 / AIU 301)
583
0
63196
Swiss-Prot
-
ARSA_CHLTE
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
405
0
45848
Swiss-Prot
-
ARSA_HALSA
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
644
0
70532
Swiss-Prot
-
ARSA_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
349
0
39919
Swiss-Prot
-
ARSA_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
324
0
36544
Swiss-Prot
-
ARSA_SYNY3
Synechocystis sp. (strain PCC 6803 / Kazusa)
396
0
44626
Swiss-Prot
-
A0A3W0FH34_SALET
586
0
63142
TrEMBL
-
Q08Z69_STIAD
Stigmatella aurantiaca (strain DW4/3-1)
651
0
70094
TrEMBL
-
A0A2W0XYG9_KLEPN
583
0
63196
TrEMBL
-
A0A5U8QTZ8_SALET
586
0
63214
TrEMBL
-
D2RWJ7_HALTV
Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 / 4k)
415
0
44410
TrEMBL
-
A0A0F6U563_MICAE
613
0
69347
TrEMBL
-
A0A6J4PRY6_9ACTN
78
0
8107
TrEMBL
-
A0A1G0D1V2_9PROT
593
0
64331
TrEMBL
-
A0A1J5R2G4_9ZZZZ
603
0
61586
TrEMBL
other Location (Reliability: 3)
A0A0B2S644_GLYSO
134
0
14653
TrEMBL
other Location (Reliability: 2)
A0A6J4MAB5_9ACTN
339
0
36512
TrEMBL
-
D6XYX5_BACIE
Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10)
587
0
63780
TrEMBL
-
D9S046_THEOJ
Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 / JW/IW-1228P)
303
0
34677
TrEMBL
-
A0A1F8YL92_9DELT
605
0
66511
TrEMBL
-
Q6MH02_BDEBA
Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100)
306
0
33854
TrEMBL
-
A0A2S8HGH0_9PSED
586
0
62743
TrEMBL
-
V6F1M0_MAGGM
Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1)
568
0
59200
TrEMBL
-
A0A1F4GEB8_9BURK
605
0
63197
TrEMBL
-
F0SJU4_RUBBR
Rubinisphaera brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / IAM 15109 / NBRC 103401 / IFAM 1448)
598
0
64042
TrEMBL
-
A0A564ZKC2_9BACT
401
0
45584
TrEMBL
-
A0A657G2A4_SALET
583
0
63126
TrEMBL
-
A0A090IYS1_9BACI
590
0
65477
TrEMBL
-
Q3B3P6_CHLL3
Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530)
396
0
44602
TrEMBL
-
Q3B5N6_CHLL3
Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530)
433
0
49262
TrEMBL
-
A0A6J4M3R6_9ACTN
387
0
40908
TrEMBL
-
Q3AU26_CHLCH
Chlorobium chlorochromatii (strain CaD3)
408
0
46275
TrEMBL
-
A0A520XGY2_9DELT
584
0
66354
TrEMBL
-
A0A6N3J6Z2_SHESW
Shewanella sp. (strain W3-18-1)
590
0
64311
TrEMBL
-
A0A6J5CU78_9BURK
588
0
63099
TrEMBL
-
A0A2N2URH1_9PROT
582
0
61154
TrEMBL
-
A1BFF2_CHLPD
Chlorobium phaeobacteroides (strain DSM 266)
395
0
44487
TrEMBL
-
A0A5E6M7W1_9BACT
584
0
62764
TrEMBL
-
A0A402DH64_MICAE
358
0
38862
TrEMBL
-
B3QL96_CHLP8
Chlorobaculum parvum (strain DSM 263 / NCIMB 8327)
394
0
44792
TrEMBL
-
Q2W688_MAGSA
Magnetospirillum magneticum (strain AMB-1 / ATCC 700264)
568
0
59780
TrEMBL
-
A9KRJ5_LACP7
Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
393
0
45025
TrEMBL
-
A9WBH2_CHLAA
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
399
0
44740
TrEMBL
-
F4BYW2_METSG
Methanothrix soehngenii (strain ATCC 5969 / DSM 3671 / JCM 10134 / NBRC 103675 / OCM 69 / GP-6)
300
0
33402
TrEMBL
-
A0A1F3SFC9_9PROT
592
0
63607
TrEMBL
-
I3R8S2_HALMT
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)
321
0
36155
TrEMBL
-
A4FAE1_SACEN
Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
400
0
42855
TrEMBL
-
Q7P866_FUSNV
388
0
44707
TrEMBL
-
R4WBU6_KLEPN
588
0
63666
TrEMBL
-
A0A8E6S297_SALER
586
0
63441
TrEMBL
-
S0G437_9DELT
304
0
34335
TrEMBL
-
A0A160T8D5_9CHLR
627
0
68312
TrEMBL
-
B8G844_CHLAD
Chloroflexus aggregans (strain MD-66 / DSM 9485)
390
0
43689
TrEMBL
-
A0A6J4HLR9_9ACTN
349
0
38122
TrEMBL
-
A0A1B4EUG5_9BURK
587
0
62572
TrEMBL
-
A0A076LZ14_9GAMM
583
0
63381
TrEMBL
-
A0A5A5RUR0_MICAE
633
0
71644
TrEMBL
-
A0A8F0CL14_SALET
586
0
63240
TrEMBL
-
A0A1G1B105_9PROT
586
0
63004
TrEMBL
-
A5HZU8_CLOBH
Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
581
0
65193
TrEMBL
-
Q21S89_ALBFT
Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
589
0
62580
TrEMBL
-
A0A1J5CAA6_9BURK
624
0
66139
TrEMBL
-
A0A0H3KRF9_BURM1
Burkholderia multivorans (strain ATCC 17616 / 249)
587
0
62490
TrEMBL
-
Q9Y9X4_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
197
0
22625
TrEMBL
-
Q9Y9X5_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
123
0
13651
TrEMBL
-
A0A850QJ61_9BURK
611
0
66445
TrEMBL
-
A0A1D8S3S3_9EURY
308
0
33647
TrEMBL
-
A0A8E6K4T4_SALET
586
0
63186
TrEMBL
-
A0A2S0PEP0_9NEIS
583
0
62115
TrEMBL
-
A0A1V4W527_9DELT
318
0
35702
TrEMBL
-
A0A5W5H4F6_SALET
586
0
63186
TrEMBL
-
A0A1U9WY92_PLAAG
395
0
44894
TrEMBL
-
A0A1F9CT60_9DELT
613
0
68684
TrEMBL
-
A0A1J0ABQ9_9CYAN
398
0
45093
TrEMBL
-
A0A1C9BM34_BACTU
393
0
44561
TrEMBL
-
A0A2W0GW31_9ENTR
583
0
62928
TrEMBL
-
B3QTL7_CHLT3
Chloroherpeton thalassium (strain ATCC 35110 / GB-78)
402
0
45116
TrEMBL
-
F8F1U8_TRECH
Treponema caldarium (strain ATCC 51460 / DSM 7334 / H1)
305
0
35134
TrEMBL
-
Q3M569_TRIV2
Trichormus variabilis (strain ATCC 29413 / PCC 7937)
395
0
44662
TrEMBL
-
A0A0H3J1I8_CLOPA
581
0
64464
TrEMBL
-
A0A1V5CIK8_9DELT
322
0
36745
TrEMBL
-
A0A0J0YNS9_9ACTN
389
0
42928
TrEMBL
-
A0A0F2NR54_9DELT
590
0
63990
TrEMBL
-
A0A5C6C0M4_9BACT
591
0
62736
TrEMBL
-
A0A0A7LC18_9ARCH
390
0
44125
TrEMBL
-
C4L6C4_EXISA
Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b)
585
0
64876
TrEMBL
-
A0A1L7FE07_9PSEU
399
0
42562
TrEMBL
-
D5EFM3_AMICL
Aminobacterium colombiense (strain DSM 12261 / ALA-1)
318
0
35716
TrEMBL
-
E3G6Q1_ENTLS
Enterobacter lignolyticus (strain SCF1)
583
0
62950
TrEMBL
-
A0A1V5CBL7_9DELT
318
0
35692
TrEMBL
-
A0A728KS12_SALET
583
0
62889
TrEMBL
-
F0SUY3_SYNGF
Syntrophobotulus glycolicus (strain DSM 8271 / FlGlyR)
578
0
62519
TrEMBL
-
A0A1V5XYT5_9FIRM
581
0
64346
TrEMBL
-
A0A6J4LFW1_9ACTN
392
0
41914
TrEMBL
-
A0A2H1KD47_BRELN
321
0
34587
TrEMBL
-
A0A2G9HKT1_9LAMI
390
0
43069
TrEMBL
Mitochondrion (Reliability: 5)
A8AC50_IGNH4
Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)
309
0
35066
TrEMBL
-
F2RAF2_STRVP
Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745)
462
0
49106
TrEMBL
-
A0A0N0MYM1_9ACTN
389
0
41909
TrEMBL
-
C9Y5U8_CROTZ
Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032)
482
0
52063
TrEMBL
-
A0A1V4YIL9_9EURY
335
0
37739
TrEMBL
-
C7RFZ2_ANAPD
Anaerococcus prevotii (strain ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806 / PC1)
580
0
64656
TrEMBL
-
Q3B680_CHLL3
Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530)
406
0
46036
TrEMBL
-
A0A1W9H1R9_9PROT
595
0
64200
TrEMBL
-
G3J256_METTV
Methylobacter tundripaludum (strain ATCC BAA-1195 / DSM 17260 / SV96)
585
0
63025
TrEMBL
-
A0A7I6QYP9_9ENTR
583
0
63363
TrEMBL
-
A0A4Z0Y8E5_9FIRM
578
0
63149
TrEMBL
-
Q1INY9_KORVE
Koribacter versatilis (strain Ellin345)
634
0
69603
TrEMBL
-
A0A8B4E8M5_9MYCO
423
0
45386
TrEMBL
-
A0A5V7YQC2_SALET
585
0
63495
TrEMBL
-
A0A1Y5DSW8_9PROT
590
0
65063
TrEMBL
-
A1BIR2_CHLPD
Chlorobium phaeobacteroides (strain DSM 266)
384
0
43017
TrEMBL
-
A0A151AR17_9CLOT
590
0
65532
TrEMBL
-
A0A5W2ACC3_SALET
586
0
63156
TrEMBL
-
M5BU04_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
105
0
11497
TrEMBL
other Location (Reliability: 1)
A0A1F4BU76_9PROT
598
0
63726
TrEMBL
-
Q5HKC0_STAEQ
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
565
0
64313
TrEMBL
-
A0A1G3I6S9_9BURK
589
0
62423
TrEMBL
-
Q3M7T7_TRIV2
Trichormus variabilis (strain ATCC 29413 / PCC 7937)
366
0
40239
TrEMBL
-
A0A644Y4Q9_9ZZZZ
202
0
22803
TrEMBL
other Location (Reliability: 1)
B3EHX8_CHLL2
Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330)
395
0
44987
TrEMBL
-
A0A1C3P813_9ACTN
404
0
42812
TrEMBL
-
A0A3Z6QFU1_SALET
586
0
63158
TrEMBL
-
A0A1T6J0G4_9MYCO
315
0
33331
TrEMBL
-
A0A1U4MKN7_9MYCO
373
0
40387
TrEMBL
-
A0A2D3JK92_FUSNV
388
0
44766
TrEMBL
-
A0A752XKJ3_SALET
586
0
63158
TrEMBL
-
A0A0K3BNE0_9PSEU
386
0
41049
TrEMBL
-
D3S1X2_FERPA
Ferroglobus placidus (strain DSM 10642 / AEDII12DO)
383
0
44346
TrEMBL
-
F2JMT5_CELLD
Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5)
389
0
44762
TrEMBL
-
F0GY97_9FIRM
580
0
65301
TrEMBL
-
A0A5X5EYX1_SALET
586
0
63140
TrEMBL
-
A0A1V4WUY6_9DELT
326
0
37308
TrEMBL
-
E6QQB0_9ZZZZ
601
0
64967
TrEMBL
other Location (Reliability: 3)
A0A1E4LY11_9PROT
584
0
62838
TrEMBL
-
A1SLC8_NOCSJ
Nocardioides sp. (strain ATCC BAA-499 / JS614)
410
0
43890
TrEMBL
-
F8C3A7_THEGP
Thermodesulfobacterium geofontis (strain OPF15)
380
0
44294
TrEMBL
-
A0A6J4TQI1_9ACTN
366
0
39098
TrEMBL
-
A0A1V4T9B5_9EURY
326
0
36657
TrEMBL
-
M1XL07_NATM8
Natronomonas moolapensis (strain DSM 18674 / CECT 7526 / JCM 14361 / 8.8.11)
643
0
70219
TrEMBL
-
I7GFH8_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
376
0
40339
TrEMBL
-
C4LKI7_CORK4
Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717)
583
0
61585
TrEMBL
-
A0A4P7CBP7_9PSEU
377
0
40455
TrEMBL
-
A0A7W8DYI1_9BRAD
586
0
62136
TrEMBL
-
A0A1Q3VVF6_9PROT
590
0
62824
TrEMBL
-
A0A732ECL1_SALET
586
0
63174
TrEMBL
-
A0A5V7YQG7_SALET
583
0
63549
TrEMBL
-
A0A3B0UMY5_9ZZZZ
49
0
5040
TrEMBL
Mitochondrion (Reliability: 5)
A0A6W0EQI6_SALET
585
0
63424
TrEMBL
-
A0A1V4XHL9_9DELT
320
0
35880
TrEMBL
-
A0A1V4WCA4_9DELT
316
0
35784
TrEMBL
-
A0A0F6QXF0_9CORY
318
0
35001
TrEMBL
-
G0HU28_HALHT
Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755)
324
0
35971
TrEMBL
-
A7MV37_VIBCB
Vibrio campbellii (strain ATCC BAA-1116 / BB120)
582
0
63447
TrEMBL
-
A0A402DC02_MICAE
395
0
44572
TrEMBL
-
A0A1E4Q7E2_MICAE
390
0
43959
TrEMBL
-
A0A0A8WZV0_9BACI
589
0
64728
TrEMBL
-
A0A1F4IZZ6_9BURK
625
0
65941
TrEMBL
-
A0A644X7J8_9ZZZZ
311
0
35063
TrEMBL
other Location (Reliability: 3)
A0A645GXB5_9ZZZZ
139
0
15536
TrEMBL
other Location (Reliability: 4)
B3EGQ4_CHLL2
Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330)
384
0
43027
TrEMBL
-
A0A5U9SEP2_SALET
583
0
63392
TrEMBL
-
Q091B7_STIAD
Stigmatella aurantiaca (strain DW4/3-1)
388
0
42008
TrEMBL
-
A0A2D3JKD5_FUSNV
396
0
45560
TrEMBL
-
A0A5J0RJJ8_SALET
586
0
63156
TrEMBL
-
A0A741FPC7_SALET
586
0
63186
TrEMBL
-
A0A5H5ZKL9_SALET
586
0
63377
TrEMBL
-
D2Z8M8_9BACT
314
0
35728
TrEMBL
-
A0A8B3S249_9EURY
311
0
34671
TrEMBL
-
C8XCW0_NAKMY
Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 / Y-104)
409
0
42836
TrEMBL
-
D6Z0Q7_DESAT
Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2)
590
0
63264
TrEMBL
-
B9SY64_RICCO
412
0
44732
TrEMBL
Chloroplast (Reliability: 1)
E3GZ72_METFV
Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S)
324
0
36890
TrEMBL
-
A4G025_METM5
Methanococcus maripaludis (strain C5 / ATCC BAA-1333)
345
0
38682
TrEMBL
-
A0A0T5ZS44_9BACT
396
0
46054
TrEMBL
-
A0A086QXW6_TOXGO
314
0
35145
TrEMBL
other Location (Reliability: 3)
A0A086QXW2_TOXGO
108
0
11991
TrEMBL
other Location (Reliability: 1)
A0A076LRL8_9GAMM
91
0
10068
TrEMBL
-
A0A7Z7LM56_9HYPH
588
0
62643
TrEMBL
-
Q18H24_HALWD
Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)
643
0
70778
TrEMBL
-
E3JBJ4_FRAIE
Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c)
445
0
47481
TrEMBL
-
A0A3S4IRP3_SALET
583
0
63078
TrEMBL
-
A0A6C6ZAJ5_SALPB
585
0
63495
TrEMBL
-
Q3L9K5_RHOE4
Rhodococcus erythropolis (strain PR4 / NBRC 100887)
585
0
62026
TrEMBL
-
C0QDL0_DESAH
Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 / HRM2)
308
0
34428
TrEMBL
-
A0A0D8FUJ4_9ACTN
286
0
30503
TrEMBL
-
A0A086CI12_9CHRO
363
0
40169
TrEMBL
-
A0A212JMK6_9PROT
577
0
60641
TrEMBL
-
A0A2K8UI26_9GAMM
582
0
60338
TrEMBL
-
A0A2N2QTY0_9PROT
581
0
60573
TrEMBL
-
B3QNY3_CHLP8
Chlorobaculum parvum (strain DSM 263 / NCIMB 8327)
395
0
44559
TrEMBL
-
A0A1V4WP39_9DELT
326
1
36779
TrEMBL
-
A4SDG8_CHLPM
Chlorobium phaeovibrioides (strain DSM 265 / 1930)
433
0
49209
TrEMBL
-
B4SFF7_PELPB
Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1)
408
0
46285
TrEMBL
-
A0A086QEQ3_TOXGO
341
0
38257
TrEMBL
Secretory Pathway (Reliability: 5)
A9WE60_CHLAA
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
390
0
43746
TrEMBL
-
D9PU08_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
324
0
36501
TrEMBL
-
A0A644W1P3_9ZZZZ
584
0
64576
TrEMBL
other Location (Reliability: 1)
A0A603N425_SALET
586
0
63142
TrEMBL
-
A0A730F9K1_SALET
586
0
63224
TrEMBL
-
A0A602VQ99_SALET
583
0
63433
TrEMBL
-
A0A6J4RMX7_9ACTN
391
0
43345
TrEMBL
-
A0A811TGA4_9EURY
311
0
34683
TrEMBL
-
A0A410UT02_9BURK
589
0
62993
TrEMBL
-
B1YC85_PYRNV
Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)
326
1
36912
TrEMBL
-
B1HYK9_LYSSC
Lysinibacillus sphaericus (strain C3-41)
586
0
65117
TrEMBL
-
A0A0C2YZD1_MAGMG
576
0
60369
TrEMBL
-
A3DKV0_STAMF
Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / JCM 9404 / F1)
329
0
37865
TrEMBL
-
A4WJA9_PYRAR
Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)
334
0
38014
TrEMBL
-
G4RMF7_THETK
Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)
333
0
38109
TrEMBL
-
A3MUH2_PYRCJ
Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)
327
1
36915
TrEMBL
-
A0A0J6VRQ7_9MYCO
340
0
35906
TrEMBL
-
A0A2N9BGD6_STRCX
391
0
41682
TrEMBL
-
A5UME7_METS3
Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS)
340
0
37891
TrEMBL
-
Q112M5_TRIEI
Trichodesmium erythraeum (strain IMS101)
626
0
70485
TrEMBL
-
A0A1F4GC09_9BURK
592
0
62400
TrEMBL
-
C9Y5U7_CROTZ
Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032)
120
0
12978
TrEMBL
-
K9ZA77_ANACC
Anabaena cylindrica (strain ATCC 27899 / PCC 7122)
395
0
44846
TrEMBL
-
A0A4P7CGM3_9PSEU
334
0
35301
TrEMBL
-
A0A1J1ADE7_9EURY
339
0
36542
TrEMBL
-
B3ENX1_CHLPB
Chlorobium phaeobacteroides (strain BS1)
433
0
49395
TrEMBL
-
A0A6C8G895_SALIN
586
0
63350
TrEMBL
-
A0A8E3WWX5_RHILT
588
0
63391
TrEMBL
-
A0A1N6C2T8_9MYCO
347
0
36644
TrEMBL
-
A0A1V4TNB5_9ARCH
370
0
42263
TrEMBL
-
M5BJ21_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
149
0
17144
TrEMBL
other Location (Reliability: 2)
A0A822LEI5_MICAE
395
0
44572
TrEMBL
-
A0A2W4RVD3_9GAMM
585
0
62346
TrEMBL
-
C7NMI6_HALUD
Halorhabdus utahensis (strain DSM 12940 / JCM 11049 / AX-2)
345
0
37808
TrEMBL
-
A0A1V5CU64_9DELT
314
0
35718
TrEMBL
-
B4SFF3_PELPB
Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1)
384
0
43073
TrEMBL
-
A9KJA6_LACP7
Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
582
0
64467
TrEMBL
-
A0A652ZXP8_9SPIR
308
0
34263
TrEMBL
-
A0A607KS95_SALET
586
0
63165
TrEMBL
-
C7P160_HALMD
Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541)
339
0
36594
TrEMBL
-
A0A644VVR5_9ZZZZ
581
0
64471
TrEMBL
other Location (Reliability: 1)
A0A644XEY8_9ZZZZ
200
0
22640
TrEMBL
other Location (Reliability: 1)
B3EGQ8_CHLL2
Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330)
405
0
45938
TrEMBL
-
A0A3V3TWT9_SALET
586
0
63266
TrEMBL
-
Q092J5_STIAD
Stigmatella aurantiaca (strain DW4/3-1)
304
0
33786
TrEMBL
-
A0A3T9Y9V1_SALET
586
0
63199
TrEMBL
-
A0A606F4Z8_SALET
586
0
63225
TrEMBL
-
A0A0F6U1Z2_MICAE
358
0
38841
TrEMBL
-
A0A5W7RU16_SALET
586
0
63159
TrEMBL
-
A0A1A9GJY5_9ACTN
333
0
35226
TrEMBL
-
A0A1A9GKG6_9ACTN
394
0
41925
TrEMBL
-
E6PKJ4_9ZZZZ
592
0
63485
TrEMBL
other Location (Reliability: 3)
A0A5X9FJH6_SALET
586
0
63142
TrEMBL
-
A0A160FXF6_9BURK
584
0
63006
TrEMBL
-
A0A0A8RV42_9ACTN
591
0
62342
TrEMBL
-
A0A1V5IAI7_9BACT
328
0
35954
TrEMBL
-
E6SD05_INTC7
Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP)
595
0
62658
TrEMBL
-
A0A1X9MHH1_9BACI
583
0
63736
TrEMBL
-
A0A7U6KGV0_9FIRM
387
0
44660
TrEMBL
-
D5SNA9_PLAL2
Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
603
0
64832
TrEMBL
-
Q3EL34_BACTI
392
0
44463
TrEMBL
-
F8D8B0_HALXS
Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6)
337
0
37486
TrEMBL
-
F2LXQ8_HIPMA
Hippea maritima (strain ATCC 700847 / DSM 10411 / MH2)
303
0
34693
TrEMBL
-
A0A658IIG1_SALNE
586
0
63170
TrEMBL
-
G2LDR5_CHLTF
Chloracidobacterium thermophilum (strain B)
420
0
46711
TrEMBL
-
A0A151AJI0_9EURY
111
0
12981
TrEMBL
-
A0A6J4KVW4_9ACTN
396
0
41829
TrEMBL
-
A0A1V6CKP1_9DELT
316
0
35784
TrEMBL
-
A0A8E6NWV7_SALET
586
0
63186
TrEMBL
-
A0A5J0I1N6_SALET
586
0
63361
TrEMBL
-
A0A5J4F7U1_MICAE
395
0
44572
TrEMBL
-
A0A3S5EVE7_9ACTN
586
0
62267
TrEMBL
-
F6BJ59_THEXL
Thermoanaerobacterium xylanolyticum (strain ATCC 49914 / DSM 7097 / LX-11)
581
0
64254
TrEMBL
-
A0A2E6P3P2_9GAMM
589
0
64107
TrEMBL
-
A0A1V5IKB9_9ACTN
786
0
81931
TrEMBL
-
Q2NHP6_METST
Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)
328
0
36921
TrEMBL
-
A0A1F4ECY8_9BURK
605
0
63116
TrEMBL
-
A0A800YL87_9ENTR
585
0
63311
TrEMBL
-
A0A801DSP2_9ENTR
583
0
63293
TrEMBL
-
A9WFY3_CHLAA
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
401
0
45100
TrEMBL
-
A0A1F4HD64_9BURK
620
0
65837
TrEMBL
-
A0A644XA15_9ZZZZ
202
0
22950
TrEMBL
other Location (Reliability: 1)
A0A645CVE4_9ZZZZ
124
0
13817
TrEMBL
other Location (Reliability: 3)
A0A3N9QLN2_9RHOB
586
0
61452
TrEMBL
-
A0A3V9E7L1_SALET
586
0
63225
TrEMBL
-
A0A0F7PAE9_9EURY
322
0
36085
TrEMBL
-
A0A5I4Y598_SALET
586
0
63331
TrEMBL
-
A0A5X9XCT0_SALET
586
0
63321
TrEMBL
-
K9XT55_STAC7
Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437)
395
0
44502
TrEMBL
-
A0A6J4PSD6_9ACTN
144
0
15950
TrEMBL
-
A0A729KXZ1_SALET
586
0
63291
TrEMBL
-
A0A735N1D8_SALET
586
0
63353
TrEMBL
-
A0A8E5MX95_SALET
586
0
63219
TrEMBL
-
A0A2M7Y5L7_9RHOO
607
0
65337
TrEMBL
-
A0A385ZT46_9ACTN
385
0
41523
TrEMBL
-
D9R5Q8_LACSW
Lacrimispora saccharolytica (strain ATCC 35040 / DSM 2544 / NRCC 2533 / WM1)
578
0
63996
TrEMBL
-
A0A7S7T4Y9_9BRAD
584
0
62517
TrEMBL
-
A0A5A5QZX3_MICAE
358
0
38856
TrEMBL
-
Q1QW02_CHRSD
Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11)
313
0
34512
TrEMBL
-
B4S3F8_PROA2
Prosthecochloris aestuarii (strain DSM 271 / SK 413)
434
0
49334
TrEMBL
-
A0A1V4ZJ38_9ARCH
306
0
34478
TrEMBL
-
A0A625AFN2_SALET
585
0
63161
TrEMBL
-
A0A6J4S5T4_9ACTN
335
0
37075
TrEMBL
-
A0A2T0AQH6_9CLOT
601
0
66643
TrEMBL
-
A0A0L6ZCL7_9CLOT
386
0
44325
TrEMBL
-
F2KME7_ARCVS
Archaeoglobus veneficus (strain DSM 11195 / SNP6)
384
0
44147
TrEMBL
-
B3EKZ5_CHLPB
Chlorobium phaeobacteroides (strain BS1)
399
0
45252
TrEMBL
-
F9ZUW5_ACICS
Acidithiobacillus caldus (strain SM-1)
600
0
64366
TrEMBL
-
F4CL41_PSEUX
Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 / CB1190)
424
0
44532
TrEMBL
-
B1I0V5_DESAP
Desulforudis audaxviator (strain MP104C)
397
0
44388
TrEMBL
-
A0A2N1ZWI1_9GAMM
583
0
63261
TrEMBL
-
A0A8B4E8E4_9MYCO
315
0
33345
TrEMBL
-
A0A1V4TDR4_9ARCH
308
0
34634
TrEMBL
-
A0A1V5CCS2_9DELT
318
0
35702
TrEMBL
-
A0A1V0LK57_9ENTR
588
0
63727
TrEMBL
-
A0A0S4HYV2_9PSED
585
0
62380
TrEMBL
-
A0A2K8PGS6_STRLA
438
0
46083
TrEMBL
-
A6URE4_METVS
Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)
345
0
38715
TrEMBL
-
A0A4D6P1B0_SALET
583
0
63392
TrEMBL
-
A0A644WJG3_9ZZZZ
578
0
62519
TrEMBL
other Location (Reliability: 1)
A0A645J4E8_9ZZZZ
85
0
9496
TrEMBL
other Location (Reliability: 1)
A0A645GW26_9ZZZZ
161
0
17803
TrEMBL
Mitochondrion (Reliability: 5)
I3RAB7_HALMT
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)
321
0
35130
TrEMBL
-
G7I505_MEDTR
406
0
44081
TrEMBL
Chloroplast (Reliability: 1)
A0A5Z2TI29_SALET
586
0
63317
TrEMBL
-
A0A315GR11_SALET
585
0
63424
TrEMBL
-
A0A0A1VXP1_MICAE
384
0
43460
TrEMBL
-
A0A8E6TZV3_SALET
586
0
63388
TrEMBL
-
F2JMT3_CELLD
Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5)
391
0
44755
TrEMBL
-
A0A1Z8LR94_9PROT
584
0
62431
TrEMBL
-
A0A0E1CSM8_KLEPN
446
0
48578
TrEMBL
-
A0A0A1H387_9BURK
590
0
63404
TrEMBL
-
A0A098E8T9_9ZZZZ
296
0
33954
TrEMBL
other Location (Reliability: 2)
M4YUM5_THEXX
Thermoplasmatales archaeon (strain BRNA1)
394
0
44258
TrEMBL
-
A0A1A9GI06_9ACTN
322
0
33872
TrEMBL
-
D0DTD4_LIMFE
564
0
62198
TrEMBL
-
A0A8B5WWD0_9GAMM
596
0
63793
TrEMBL
-
A0A7U4DNW5_DESPD
Desulfobulbus propionicus (strain ATCC 33891 / DSM 2032 / VKM B-1956 / 1pr3)
600
0
64889
TrEMBL
-
A0A5X6EPV3_SALET
586
0
63240
TrEMBL
-
A0A1Y6BX54_9NEIS
612
0
65653
TrEMBL
-
Q1H178_METFK
Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875)
587
0
62841
TrEMBL
-
A0A6J4JF24_9ACTN
391
0
37225
TrEMBL
-
E0UHF9_GLOV7
Gloeothece verrucosa (strain PCC 7822)
395
0
44757
TrEMBL
-
A0A0H3BPY3_SALNS
Salmonella newport (strain SL254)
586
0
63170
TrEMBL
-
A0A5A5S5B4_MICAE
633
0
71651
TrEMBL
-
A0A4Q9US82_9GAMM
587
0
62546
TrEMBL
-
G2LHF1_CHLTF
Chloracidobacterium thermophilum (strain B)
374
0
40985
TrEMBL
-
G2LEX7_CHLTF
Chloracidobacterium thermophilum (strain B)
395
0
44254
TrEMBL
-
S0FR17_RUMCE
386
0
44102
TrEMBL
-
C9YA76_CURXX
Curvibacter symbiont subsp. Hydra magnipapillata
590
0
62224
TrEMBL
-
F6DK49_DESRL
Desulforamulus ruminis (strain ATCC 23193 / DSM 2154 / NCIMB 8452 / DL)
587
0
64430
TrEMBL
-
A0A1Y2NMH5_STRFR
505
0
52500
TrEMBL
-
A0A0A1U2U5_ENTIV
328
0
36674
TrEMBL
other Location (Reliability: 1)
D3SLF0_THEAH
Thermocrinis albus (strain DSM 14484 / JCM 11386 / HI 11/12)
408
0
46832
TrEMBL
-
A0A0C2BHI2_9BURK
587
0
63370
TrEMBL
-
M2XPH9_GALSU
706
0
79398
TrEMBL
other Location (Reliability: 3)
C7P7U9_METFA
Methanocaldococcus fervens (strain DSM 4213 / JCM 15782 / AG86)
345
0
39264
TrEMBL
-
W6RHD6_PSEP5
Pseudomonas pseudoalcaligenes (strain CECT 5344)
584
0
62674
TrEMBL
-
A0A645ARC7_9ZZZZ
361
0
41376
TrEMBL
other Location (Reliability: 2)
A0A2P2BW51_9ZZZZ
400
0
42743
TrEMBL
other Location (Reliability: 3)
A0A3V3B7I9_SALET
586
0
63163
TrEMBL
-
B7PS86_IXOSC
343
0
38229
TrEMBL
other Location (Reliability: 4)
D2RRB0_HALTV
Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 / 4k)
332
0
36272
TrEMBL
-
A0A2N9MH42_9BACT
395
0
44519
TrEMBL
-
A0A1V4XLB6_9DELT
316
0
36200
TrEMBL
-
A0A6J4SZE3_9ACTN
402
0
44385
TrEMBL
-
A0A812A199_9EURY
311
0
34676
TrEMBL
-
A0A1J5BKB6_9PROT
607
0
65337
TrEMBL
-
A0A075MVB0_9ARCH
391
0
42994
TrEMBL
-
A7GBE7_CLOBL
Clostridium botulinum (strain Langeland / NCTC 10281 / Type F)
581
0
65302
TrEMBL
-
A0A6J4IBU3_9ACTN
389
0
42583
TrEMBL
-
A0A7Z2PVM6_9BRAD
584
0
62145
TrEMBL
-
G5R1Q7_SALSE
586
0
63351
TrEMBL
-
K7RTL1_ACIA4
Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070 / 4)
588
0
62440
TrEMBL
-
A6TP82_ALKMQ
Alkaliphilus metalliredigens (strain QYMF)
295
0
33103
TrEMBL
-
A0A0E2BXC5_LACCA
577
0
63781
TrEMBL
-
A0A2M7F110_9RHOB
584
0
61585
TrEMBL
-
A0A6J4NB88_9ACTN
392
0
42249
TrEMBL
-
Q11AD6_TRIEI
Trichodesmium erythraeum (strain IMS101)
395
0
44722
TrEMBL
-
A0A344UQA8_9ACTN
599
0
62993
TrEMBL
-
A0A7I6U4Y6_9ENTR
583
0
63381
TrEMBL
-
A0A059KH79_9BURK
585
0
61679
TrEMBL
-
D2Q091_KRIFD
Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399)
432
0
47153
TrEMBL
-
A0A1F3AM13_9PROT
589
0
62107
TrEMBL
-
A0A1V6HHN0_9BACT
293
0
31062
TrEMBL
-
A0A6J4S5I6_9ACTN
395
0
40740
TrEMBL
-
A0A519BDK9_9DELT
584
0
66039
TrEMBL
-
A0A3P3ZWB3_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
409
0
44001
TrEMBL
-
A4YC51_SHEPC
Shewanella putrefaciens (strain CN-32 / ATCC BAA-453)
588
0
63923
TrEMBL
-
B8HL64_CYAP4
Cyanothece sp. (strain PCC 7425 / ATCC 29141)
394
0
44251
TrEMBL
-
A0A5Q5BLZ5_MYCSS
Mycobacterium sp. (strain MCS)
421
0
44845
TrEMBL
-
A0A2N2QN06_9PROT
597
0
62729
TrEMBL
-
L7JWR1_TRAHO
390
0
44608
TrEMBL
other Location (Reliability: 2)
A0A2H1K8A4_9MICO
343
0
37554
TrEMBL
-
A0A1F4E3Q0_9PROT
607
0
64118
TrEMBL
-
A0A5C1QA58_9BURK
584
0
61485
TrEMBL
-
A0A086CHY9_9CHRO
397
0
44787
TrEMBL
-
A2RKM7_LACLM
Lactococcus lactis subsp. cremoris (strain MG1363)
571
0
63397
TrEMBL
-
A6LV97_CLOB8
Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052)
582
0
64791
TrEMBL
-
A0A0P8A3W5_9EURY
625
0
70860
TrEMBL
-
A0A1B7JJC7_9GAMM
582
0
63702
TrEMBL
-
G0HVV9_HALHT
Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755)
311
0
33901
TrEMBL
-
A0A5Q0BHQ4_9GAMM
584
0
62416
TrEMBL
-
A8MGW2_ALKOO
Alkaliphilus oremlandii (strain OhILAs)
582
0
64515
TrEMBL
-
A0A6C8LU66_SALET
586
0
63224
TrEMBL
-
A0A0H3CDX9_ENTCC
Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56)
588
0
63769
TrEMBL
-
A9WBH6_CHLAA
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
407
0
45356
TrEMBL
-
A0A1Q9N7X6_ODILC
Odinarchaeota archaeon (strain LCB_4)
319
0
35568
TrEMBL
-
A0A0S3QVT8_THET7
Thermosulfidibacter takaii (strain DSM 17441 / JCM 13301 / NBRC 103674 / ABI70S6)
305
0
34931
TrEMBL
-
B3QVP8_CHLT3
Chloroherpeton thalassium (strain ATCC 35110 / GB-78)
434
0
49361
TrEMBL
-
A0A5J2KGV1_SALET
583
0
63027
TrEMBL
-
A0A605YHU2_SALET
586
0
63158
TrEMBL
-
A0A0F6RN68_MICAE
384
0
43426
TrEMBL
-
A0A8E6NKD4_SALET
586
0
63186
TrEMBL
-
A0A6J4PVA7_9ACTN
390
0
42932
TrEMBL
-
A0A811TB73_9EURY
311
0
34675
TrEMBL
-
A0A424WC30_ALCXX
594
0
63265
TrEMBL
-
A0A329VEJ3_9GAMM
594
0
64870
TrEMBL
-
B8G5W5_CHLAD
Chloroflexus aggregans (strain MD-66 / DSM 9485)
404
0
45357
TrEMBL
-
Q0ABX0_ALKEH
Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1)
318
0
35997
TrEMBL
-
B8DIN3_DESVM
Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F)
579
0
62936
TrEMBL
-
A0A2M7CDS5_9DELT
601
0
67945
TrEMBL
-
D9RAP4_LACSW
Lacrimispora saccharolytica (strain ATCC 35040 / DSM 2544 / NRCC 2533 / WM1)
578
0
63470
TrEMBL
-
C1FUI9_CLOBJ
Clostridium botulinum (strain Kyoto / Type A2)
581
0
65087
TrEMBL
-
A0A2N9BA01_STRCX
471
0
50214
TrEMBL
-
E6QJN7_9ZZZZ
607
0
64903
TrEMBL
other Location (Reliability: 2)
A0A0L6JW34_9FIRM
388
0
44140
TrEMBL
-
B4S8I8_PROA2
Prosthecochloris aestuarii (strain DSM 271 / SK 413)
397
0
44536
TrEMBL
-
A0A073CR77_PLAAG
364
0
39810
TrEMBL
-
M1SJG2_MORMO
583
0
63494
TrEMBL
-
D5U1R4_THEAM
Thermosphaera aggregans (strain DSM 11486 / M11TL)
317
0
35648
TrEMBL
-
A0A2N2FR81_9DELT
620
0
69219
TrEMBL
-
Q7ULE5_RHOBA
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
593
0
64198
TrEMBL
-
H6QCM3_PYROT
Pyrobaculum oguniense (strain DSM 13380 / JCM 10595 / TE7)
301
0
33625
TrEMBL
-
A0A5X3P9E6_SALET
583
0
63126
TrEMBL
-
M1Q346_BACTU
393
0
44579
TrEMBL
-
A0A1V6IA37_9DELT
326
1
37218
TrEMBL
-
A0A5Y7ACV4_SALIN
586
0
63350
TrEMBL
-
A0A4P7C869_9PSEU
308
0
33181
TrEMBL
-
B3ENL4_CHLPB
Chlorobium phaeobacteroides (strain BS1)
405
0
45955
TrEMBL
-
E8T5Q8_THEA1
Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1)
290
0
32201
TrEMBL
-
A0A1N1SKR6_9MYCO
423
0
45400
TrEMBL
-
A0A087CKY3_9BIFI
594
0
63813
TrEMBL
-
A0A212IXA0_9FIRM
578
0
62294
TrEMBL
-
A0A2I8TMS9_9ENTR
583
0
63397
TrEMBL
-
B2IZ19_NOSP7
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
395
0
44668
TrEMBL
-
A0A8B4DEN3_9MYCO
423
0
45415
TrEMBL
-
A4JMY5_BURVG
Burkholderia vietnamiensis (strain G4 / LMG 22486)
587
0
62279
TrEMBL
-
M2XUU5_GALSU
757
0
85343
TrEMBL
Mitochondrion (Reliability: 2)
B3QR42_CHLP8
Chlorobaculum parvum (strain DSM 263 / NCIMB 8327)
384
0
43060
TrEMBL
-
A0A644XAU1_9ZZZZ
579
0
64131
TrEMBL
other Location (Reliability: 1)
A0A2P2CDV4_9ZZZZ
403
0
43502
TrEMBL
Mitochondrion (Reliability: 2)
A0A5U9SC51_SALET
585
0
63506
TrEMBL
-
Q8RIN3_FUSNN
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355)
396
0
45504
TrEMBL
-
G4SZS0_META2
Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z)
335
0
37140
TrEMBL
-
A0A0K3BHF4_9PSEU
323
0
33960
TrEMBL
-
D2R960_PIRSD
Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128)
593
0
63225
TrEMBL
-
A0A1G3UM50_9DELT
613
0
68651
TrEMBL
-
A0A8B2S714_9ENTR
583
0
63409
TrEMBL
-
Q0A537_ALKEH
Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1)
571
0
61424
TrEMBL
-
B8G7V3_CHLAD
Chloroflexus aggregans (strain MD-66 / DSM 9485)
399
0
44773
TrEMBL
-
A0A0E1CMG1_KLEPN
187
0
20578
TrEMBL
-
A0A6J4H0U4_9ACTN
347
0
37498
TrEMBL
-
A0A447JGC1_SALET
586
0
63240
TrEMBL
-
A6TP83_ALKMQ
Alkaliphilus metalliredigens (strain QYMF)
296
0
33463
TrEMBL
-
A0A512HJ41_9HYPH
588
0
62890
TrEMBL
-
A0A132MLP6_9ACTN
328
0
35050
TrEMBL
-
A0A6J4MD06_9ACTN
422
0
45368
TrEMBL
-
A0A7U6KGJ2_9FIRM
392
0
44770
TrEMBL
-
A0A1V5XIK1_9DELT
314
0
34508
TrEMBL
-
A0A2H9ZUZ8_9ASPA
384
0
42197
TrEMBL
Mitochondrion (Reliability: 4)
A0A1V5WXV6_9DELT
297
0
31841
TrEMBL
-
J0V5L4_RHIL1
Rhizobium leguminosarum bv. viciae (strain WSM1455)
588
0
63461
TrEMBL
-
K9ZA53_CYAAP
Cyanobacterium aponinum (strain PCC 10605)
393
0
44475
TrEMBL
-
A0A1Q3VTL7_9PROT
583
0
62099
TrEMBL
-
A0A257FME8_9BURK
587
0
61905
TrEMBL
-
A0A1V6ECR5_9PROT
271
0
29053
TrEMBL
-
A0A068VV44_PROFF
591
0
62499
TrEMBL
-
A0A1M9E3X9_9MYCO
347
0
36630
TrEMBL
-
A1BD03_CHLPD
Chlorobium phaeobacteroides (strain DSM 266)
392
0
44286
TrEMBL
-
A0A1A8XID5_9RHOO
600
0
63922
TrEMBL
-
A0A259V0S3_9FIRM
596
0
65457
TrEMBL
-
B7NED5_ECOLU
Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
591
0
64439
TrEMBL
-
A0A068MU76_SYNY4
395
0
44474
TrEMBL
-
Q2J8E1_FRACC
Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3)
404
0
42933
TrEMBL
-
B3QR38_CHLP8
Chlorobaculum parvum (strain DSM 263 / NCIMB 8327)
405
0
45935
TrEMBL
-
A4SCZ5_CHLPM
Chlorobium phaeovibrioides (strain DSM 265 / 1930)
384
0
42954
TrEMBL
-
A0A1L3GMS5_9DELT
575
0
61301
TrEMBL
-
G5Q488_SALMO
586
0
63395
TrEMBL
-
D6CMG7_THIA3
Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As)
592
0
63542
TrEMBL
-
F2NHZ5_DESAR
Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2)
653
0
73096
TrEMBL
-
C6W9H6_ACTMD
Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101)
406
0
42146
TrEMBL
-
B3QS08_CHLT3
Chloroherpeton thalassium (strain ATCC 35110 / GB-78)
405
0
45126
TrEMBL
-
A0A644T9D9_9ZZZZ
567
0
62332
TrEMBL
Mitochondrion (Reliability: 5)
A0A645I5W3_9ZZZZ
128
0
14672
TrEMBL
other Location (Reliability: 2)
E6SKW1_THEM7
Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a)
338
0
38365
TrEMBL
-
A8D7Y4_STREQ
580
0
63705
TrEMBL
-
A0A0D6IRH3_ALCXX
594
0
63295
TrEMBL
-
A0A2T8X9J7_SALET
586
0
63388
TrEMBL
-
A0A3V5VXI6_SALET
586
0
63142
TrEMBL
-
Q8RIN4_FUSNN
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355)
388
0
44863
TrEMBL
-
A0A160SZ56_9CHLR
398
0
43915
TrEMBL
-
D7DQT1_METV3
Methanococcus voltae (strain ATCC BAA-1334 / A3)
343
0
38378
TrEMBL
-
A6TLY6_ALKMQ
Alkaliphilus metalliredigens (strain QYMF)
296
0
33462
TrEMBL
-
A0A073CKS1_PLAAG
631
0
71262
TrEMBL
-
A0A5J6VWK6_9PROT
588
0
62961
TrEMBL
-
Q4UCT5_THEAN
318
0
36359
TrEMBL
other Location (Reliability: 1)
U5MPD6_CLOSA
581
0
64896
TrEMBL
-
A0R917_BACAH
Bacillus thuringiensis (strain Al Hakam)
393
0
44512
TrEMBL
-
A0A060HJ98_9ARCH
391
0
42712
TrEMBL
-
A0A844B4J0_9BURK
592
0
62119
TrEMBL
-
F8E589_FLESM
Flexistipes sinusarabici (strain ATCC 49648 / DSM 4947 / MAS 10)
303
0
34598
TrEMBL
-
A0A6J4S8B2_9ACTN
371
0
38923
TrEMBL
-
Q6KZR9_PICTO
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
386
0
43984
TrEMBL
-
I7G4P9_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
425
0
45301
TrEMBL
-
A6VIF3_METM7
Methanococcus maripaludis (strain C7 / ATCC BAA-1331)
345
0
38886
TrEMBL
-
A0A5I0D228_SALET
586
0
63288
TrEMBL
-
A0A7R9NEC0_9EURY
397
0
46056
TrEMBL
-
F8ALS1_METOI
Methanothermococcus okinawensis (strain DSM 14208 / JCM 11175 / IH1)
357
0
40569
TrEMBL
-
B3EQN0_CHLPB
Chlorobium phaeobacteroides (strain BS1)
398
0
44758
TrEMBL
-
A0A2S0QWR1_9RHOO
589
0
62352
TrEMBL
-
A0A2A2IWX0_9PSED
586
0
62671
TrEMBL
-
A0A6J4KSV7_9ACTN
404
0
42888
TrEMBL
-
K9TTB3_CHRTP
Chroococcidiopsis thermalis (strain PCC 7203)
395
0
44813
TrEMBL
-
A0A3B0SA17_9ZZZZ
590
0
62980
TrEMBL
other Location (Reliability: 4)
A0A377YUX7_KLEPN
191
0
20907
TrEMBL
-
D5VSQ1_METIM
Methanocaldococcus infernus (strain DSM 11812 / JCM 15783 / ME)
332
0
38042
TrEMBL
-
H6LGJ3_ACEWD
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
386
0
43815
TrEMBL
-
A0A223ZHB0_9EURY
324
0
36544
TrEMBL
-
A0A1V4WQ85_9DELT
326
0
37366
TrEMBL
-
A0A484IEK4_9ARCH
392
0
44510
TrEMBL
-
A1VTP9_POLNA
Polaromonas naphthalenivorans (strain CJ2)
600
0
63214
TrEMBL
-
B3EIV1_CHLL2
Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330)
397
0
44840
TrEMBL
-
A0A5W0N028_SALET
586
0
63300
TrEMBL
-
A0A0F7P7N9_9EURY
343
0
37338
TrEMBL
-
A0A486X6K3_SALET
586
0
63158
TrEMBL
-
Q7P865_FUSNV
331
0
38925
TrEMBL
-
A0A0A1W079_MICAE
358
0
38956
TrEMBL
-
A0A2H5Y944_9CHLR
252
0
29706
TrEMBL
-
A0A1V6EB58_9SPIR
310
0
35062
TrEMBL
-
B1YC84_PYRNV
Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta)
334
0
38075
TrEMBL
-
A0A1X1FB66_9LACO
577
0
63745
TrEMBL
-
A0A0C2YTF7_MAGMG
584
0
61383
TrEMBL
-
A0A602UR71_SALET
586
0
63353
TrEMBL
-
A4WJA8_PYRAR
Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6)
327
0
36760
TrEMBL
-
A0A855LXJ3_9ENTR
583
0
63381
TrEMBL
-
A0A2N9B9Z8_STRCX
325
0
35012
TrEMBL
-
C5A5D5_THEGJ
Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3)
336
0
38729
TrEMBL
-
A6TNA8_ALKMQ
Alkaliphilus metalliredigens (strain QYMF)
391
0
44926
TrEMBL
-
A0A1V4ZB65_9ARCH
398
0
45950
TrEMBL
-
D2RGH0_ARCPA
Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18)
382
0
44336
TrEMBL
-
A0A6J4JRY5_9ACTN
379
0
38926
TrEMBL
-
A0A8G2J296_RHILV
588
0
63401
TrEMBL
-
A0A6J4RRP2_9ACTN
168
0
18082
TrEMBL
-
I7FME3_MYCS2
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
344
0
36835
TrEMBL
-
A0A0L6ZCM7_9CLOT
388
0
44873
TrEMBL
-
A0A1V4Z7X4_9ARCH
395
0
44799
TrEMBL
-
A0A151AJE6_9EURY
196
0
20817
TrEMBL
-
A0A2H1IBV5_9MICO
320
0
34659
TrEMBL
-
A0A6J4LFY3_9ACTN
407
0
42939
TrEMBL
-
Q3AU30_CHLCH
Chlorobium chlorochromatii (strain CaD3)
385
0
43226
TrEMBL
-
Q3AQT9_CHLCH
Chlorobium chlorochromatii (strain CaD3)
396
0
44707
TrEMBL
-
A0A0D8FSW4_9ACTN
308
0
33203
TrEMBL
-
Q01U14_SOLUE
Solibacter usitatus (strain Ellin6076)
395
0
44586
TrEMBL
-
A0A5J4F2T3_MICAE
633
0
71807
TrEMBL
-
A0A1Q3S9S7_9BURK
605
0
63125
TrEMBL
-
A0A5Q5CIB4_MYCSJ
Mycobacterium sp. (strain JLS)
421
0
44845
TrEMBL
-
A0A2U3QE12_9BACT
606
0
68526
TrEMBL
-
A1TFB6_MYCVP
Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1)
729
0
77043
TrEMBL
-
A0A068N3H3_SYNY4
362
0
39204
TrEMBL
-
B3QQ79_CHLP8
Chlorobaculum parvum (strain DSM 263 / NCIMB 8327)
433
0
49127
TrEMBL
-
A0A1G0ETN1_9PROT
593
0
64331
TrEMBL
-
A0A1Q9NYW6_THOAA
Thorarchaeota archaeon (strain AB_25)
369
0
40485
TrEMBL
-
A0A644X860_9ZZZZ
579
0
64337
TrEMBL
other Location (Reliability: 2)
A0A3V7PBB2_SALET
586
0
63353
TrEMBL
-
A0A8E6KGR2_SALET
583
0
62889
TrEMBL
-
A0A6J4JZB7_9PSEU
uncultured Actinomycetospora sp
273
0
28828
TrEMBL
-
D2B4X8_STRRD
Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100)
389
0
41849
TrEMBL
-
A0A1F4K3U8_9BURK
594
0
63052
TrEMBL
-
A0A2T7UF46_9BURK
587
0
62831
TrEMBL
-
A0A1M3JUE2_9BURK
594
0
63675
TrEMBL
-
A0A753FV96_SALET
586
0
63441
TrEMBL
-
A0A1J5QJR8_9ZZZZ
590
0
63427
TrEMBL
Mitochondrion (Reliability: 5)
E6QVM0_9ZZZZ
601
0
64831
TrEMBL
other Location (Reliability: 4)
A6TLY5_ALKMQ
Alkaliphilus metalliredigens (strain QYMF)
295
0
33154
TrEMBL
-
D8GTI1_CLOLD
Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC)
581
0
64667
TrEMBL
-
B4S3T3_PROA2
Prosthecochloris aestuarii (strain DSM 271 / SK 413)
395
0
44750
TrEMBL
-
A0A6J4LVE3_9ACTN
401
0
42187
TrEMBL
-
A0A6J4MY79_9ACTN
391
0
41913
TrEMBL
-
A0A2G9GYH7_9LAMI
410
0
44805
TrEMBL
Chloroplast (Reliability: 2)
A0A1F8XGE8_9DELT
622
0
67079
TrEMBL
-
B8BXZ3_THAPS
323
0
35821
TrEMBL
other Location (Reliability: 3)
D8K2C4_DEHLB
Dehalogenimonas lykanthroporepellens (strain ATCC BAA-1523 / JCM 15061 / BL-DC-9)
408
0
46166
TrEMBL
-
A9A8D1_METM6
Methanococcus maripaludis (strain C6 / ATCC BAA-1332)
344
0
38531
TrEMBL
-
A0A5I9BGG8_SALET
586
0
63271
TrEMBL
-
Q3AQQ5_CHLCH
Chlorobium chlorochromatii (strain CaD3)
434
0
49531
TrEMBL
-
A0A3B0UB18_9ZZZZ
300
0
34457
TrEMBL
other Location (Reliability: 2)
G5NEN6_SALET
586
0
63240
TrEMBL
-
A0A1Y2NMI0_STRFR
338
0
35771
TrEMBL
-
A0A377YUX0_KLEPN
207
0
22897
TrEMBL
-
B2IVS9_NOSP7
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
366
0
39972
TrEMBL
-
A0A1N4YHJ5_9MYCO
423
0
45372
TrEMBL
-
A0A518L338_9BACT
599
0
63756
TrEMBL
-
C1D598_LARHH
Laribacter hongkongensis (strain HLHK9)
433
0
45250
TrEMBL
-
A4SE89_CHLPM
Chlorobium phaeovibrioides (strain DSM 265 / 1930)
396
0
44532
TrEMBL
-
B4SGH2_PELPB
Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1)
407
0
45999
TrEMBL
-
A0A1V5CL79_9DELT
326
1
37344
TrEMBL
-
A0A086QER0_TOXGO
85
0
9181
TrEMBL
other Location (Reliability: 1)
B7KDX9_GLOC7
Gloeothece citriformis (strain PCC 7424)
394
0
44536
TrEMBL
-
A0A1J5DIY8_9DELT
619
0
66739
TrEMBL
-
B3ECK8_CHLL2
Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330)
400
0
45294
TrEMBL
-
B3EE50_CHLL2
Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330)
396
0
45008
TrEMBL
-
A0A5H6F724_SALET
586
0
63313
TrEMBL
-
A0A2I5THR7_SERS3
Serratia sp. (strain ATCC 39006)
583
0
63469
TrEMBL
-
A0A6J4R2B3_9ACTN
393
0
43744
TrEMBL
-
F4KML3_PORAD
Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC 10618 / JCM 6326 / LMG 13178 / VPI 4198)
572
0
63445
TrEMBL
-
A0A1V4I751_9FIRM
581
0
64821
TrEMBL
-
A0A8B6GF91_MYTGA
243
0
27607
TrEMBL
other Location (Reliability: 2)
A0A2P9IHR4_9ACTN
333
0
35598
TrEMBL
-
A0A0J6VZZ9_9MYCO
413
0
44264
TrEMBL
-
A0A4P9UTR0_9GAMM
585
0
63571
TrEMBL
-
A0A2P6P5Q3_ROSCH
52
0
5202
TrEMBL
Secretory Pathway (Reliability: 5)
Q31NT0_SYNE7
Synechococcus elongatus (strain PCC 7942 / FACHB-805)
392
0
44139
TrEMBL
-
A0A5A5RH21_MICAE
395
0
44580
TrEMBL
-
B4S528_PROA2
Prosthecochloris aestuarii (strain DSM 271 / SK 413)
405
0
45789
TrEMBL
-
A1JPZ3_YERE8
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
583
0
63201
TrEMBL
-
A0A625AIE8_SALET
583
0
63228
TrEMBL
-
A6TI78_KLEP7
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
583
0
63196
TrEMBL
-
A0A1H5I2I4_9PSED
585
0
62524
TrEMBL
-
A0A8E7V1S6_SALET
586
0
63228
TrEMBL
-
A0A737H9E4_SALER
586
0
63034
TrEMBL
-
A0A140NI13_PROSM
Providencia stuartii (strain MRSN 2154)
583
0
63481
TrEMBL
-
B2J651_NOSP7
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
623
0
70049
TrEMBL
-
A0A2N2TCT4_9PROT
613
0
64410
TrEMBL
-
A0A2M8BPI6_9BURK
624
0
66037
TrEMBL
-
A0A7S7UTM2_9BRAD
584
0
62532
TrEMBL
-
A1BIR6_CHLPD
Chlorobium phaeobacteroides (strain DSM 266)
405
0
45911
TrEMBL
-
A1BEA6_CHLPD
Chlorobium phaeobacteroides (strain DSM 266)
433
0
49338
TrEMBL
-
A0A1Q9NED1_9ARCH
318
0
35703
TrEMBL
-
C9RFN3_METVM
Methanocaldococcus vulcanius (strain ATCC 700851 / DSM 12094 / M7)
363
0
41564
TrEMBL
-
A0A1E4QGA7_MICAE
358
0
38888
TrEMBL
-
Q2RUE7_RHORT
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)
571
0
59170
TrEMBL
-
A0A0A8X8L2_9BACI
319
0
36206
TrEMBL
-
B4SDP4_PELPB
Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1)
433
0
49262
TrEMBL
-
B4SA74_PELPB
Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1)
395
0
44620
TrEMBL
-
B3QV95_CHLT3
Chloroherpeton thalassium (strain ATCC 35110 / GB-78)
405
0
45541
TrEMBL
-
A0A1G0DUK0_9PROT
584
0
62365
TrEMBL
-
A0A644WFG6_9ZZZZ
580
0
64313
TrEMBL
other Location (Reliability: 1)
I3R2E6_HALMT
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)
404
0
43941
TrEMBL
-
T0QYI5_AERSA
599
0
63873
TrEMBL
-
A0A730JKC0_SALET
586
0
63397
TrEMBL
-
A0A726RZQ5_SALET
586
0
63298
TrEMBL
-
A0A385ZL52_9ACTN
447
0
48158
TrEMBL
-
A0A1F4DVK1_9PROT
595
0
63347
TrEMBL
-
A0A0J6YH04_9MYCO
376
0
40322
TrEMBL
-
A3MUH1_PYRCJ
Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)
334
0
37977
TrEMBL
-
A0A1J5S0Z0_9ZZZZ
592
0
63096
TrEMBL
other Location (Reliability: 3)
A0A1V4ZCH6_9ARCH
330
0
36576
TrEMBL
-
M9SCS3_METAX
Methanomethylophilus alvus (strain Mx1201)
390
0
43897
TrEMBL
-
F2RAF1_STRVP
Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745)
326
0
34656
TrEMBL
-
A0A248VVR3_9BURK
590
0
63557
TrEMBL
-
A0A1R4KFV1_9MICO
323
0
34825
TrEMBL
-
A0A151AIT4_9EURY
358
0
38671
TrEMBL
-
A0A807Z7C7_AERSA
599
0
63873
TrEMBL
-
A4T7G2_MYCGI
Mycolicibacterium gilvum (strain PYR-GCK)
589
0
62598
TrEMBL
-
D9SJY5_GALCS
Gallionella capsiferriformans (strain ES-2)
582
0
62800
TrEMBL
-
A0A3B0R870_9ZZZZ
392
0
43896
TrEMBL
Mitochondrion (Reliability: 3)
V7IHR7_SALET
586
0
63256
TrEMBL
-
A0A1G0AS29_9PROT
582
0
62980
TrEMBL
-
A1BFV4_CHLPD
Chlorobium phaeobacteroides (strain DSM 266)
407
0
46363
TrEMBL
-
A0A151B6C2_9CLOT
314
0
35746
TrEMBL
-
A0A1F3BNB9_9DELT
592
0
62685
TrEMBL
-
H6LGJ2_ACEWD
Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1)
388
0
44600
TrEMBL
-
A0A1J0AFH2_9CYAN
350
0
39297
TrEMBL
-
A0A2D2D0A5_METTR
589
0
62584
TrEMBL
-
A0A5W8XAC8_SALET
586
0
63244
TrEMBL
-
D3S3N9_METSF
Methanocaldococcus sp. (strain FS406-22)
349
0
39963
TrEMBL
-
A0A2I8QKH9_9ENTR
588
0
63769
TrEMBL
-
A0A1U7M3X4_TISCR
537
0
59877
TrEMBL
-
A0A702BAW1_SALET
586
0
63353
TrEMBL
-
A0A4Q8PIZ4_SALET
586
0
63256
TrEMBL
-
A0A3V8PIM6_SALET
586
0
63224
TrEMBL
-
A0A072UVY6_MEDTR
381
0
41654
TrEMBL
Chloroplast (Reliability: 5)
A0A2I8SEX5_9ENTR
583
0
63381
TrEMBL
-
A0A3V2S525_SALET
586
0
63164
TrEMBL
-
A0A315I1F7_SALET
583
0
63364
TrEMBL
-
A0A2T9I501_SALET
586
0
63385
TrEMBL
-
A0A5T5IBZ1_SALET
586
0
63186
TrEMBL
-
A0A259MF89_9PROT
589
0
62482
TrEMBL
-
A7NJJ3_ROSCS
Roseiflexus castenholzii (strain DSM 13941 / HLO8)
396
0
44256
TrEMBL
-
D2RLF5_ACIFV
Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4)
577
0
63284
TrEMBL
-
A0A8E6J9V9_SALNE
586
0
63170
TrEMBL
-
A0A6J4GYT9_9ACTN
318
0
34289
TrEMBL
-
A0A2H9T5E3_9ZZZZ
582
0
63827
TrEMBL
other Location (Reliability: 5)
A0A727UAA1_SALET
586
0
63385
TrEMBL
-
A0A728QU99_SALET
585
0
63524
TrEMBL
-
A0A6J4LLP1_9ACTN
355
0
37728
TrEMBL
-
Q5UZC1_HALMA
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
426
0
47110
TrEMBL
-
A0A6J4SR29_9ACTN
385
0
40147
TrEMBL
-
A0A519BLK7_9DELT
658
0
74765
TrEMBL
-
A0A0L6Z9Z1_9CLOT
581
0
64849
TrEMBL
-
S0FR71_RUMCE
388
0
44434
TrEMBL
-
A0A151AI58_9EURY
314
0
35161
TrEMBL
-
A0A1Q3R328_9BURK
588
0
62433
TrEMBL
-
Q3B676_CHLL3
Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530)
384
0
42945
TrEMBL
-
A0A1V6HX56_9DELT
321
0
35431
TrEMBL
-
Q3AUD0_CHLCH
Chlorobium chlorochromatii (strain CaD3)
401
0
45201
TrEMBL
-
A0A0P8AJN5_9EURY
302
0
34001
TrEMBL
-
F1TD41_9FIRM
386
0
43870
TrEMBL
-
D7GG35_PROFC
Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1)
591
0
62499
TrEMBL
-
A0A1T7V6K4_9MYCO
315
0
33361
TrEMBL
-
A0A1T7JPZ5_9MYCO
423
0
45457
TrEMBL
-
G8TTU2_SULAD
Sulfobacillus acidophilus (strain ATCC 700253 / DSM 10332 / NAL)
307
0
33798
TrEMBL
-
A0A1F4JHY6_9BURK
591
0
62628
TrEMBL
-
A1TAZ1_MYCVP
Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1)
430
0
46033
TrEMBL
-
A0A258RHT5_9BURK
615
0
64966
TrEMBL
-
A0A4D6P2F8_SALET
585
0
63506
TrEMBL
-
A0A644X0V4_9ZZZZ
572
0
63453
TrEMBL
other Location (Reliability: 2)
A0A644TYJ7_9ZZZZ
336
0
37178
TrEMBL
other Location (Reliability: 3)
A0A073CKZ8_PLAAG
395
0
44894
TrEMBL
-
A0A3V4SMV3_SALET
586
0
63244
TrEMBL
-
Q0AYF1_SYNWW
Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)
583
0
64131
TrEMBL
-
A0A6J4RS63_9ACTN
311
0
32331
TrEMBL
-
B0RA87_HALS3
Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
644
0
70532
TrEMBL
-
A0A1A9GNS6_9ACTN
402
0
43021
TrEMBL
-
A0A2P9IHP0_9ACTN
375
0
40630
TrEMBL
-
L1LAK4_THEEQ
268
0
30682
TrEMBL
other Location (Reliability: 1)
B4S524_PROA2
Prosthecochloris aestuarii (strain DSM 271 / SK 413)
384
0
42760
TrEMBL
-
A9B8G0_HERA2
Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95)
391
0
43565
TrEMBL
-
K9YK61_CYASC
Cyanobacterium stanieri (strain ATCC 29140 / PCC 7202)
388
0
43883
TrEMBL
-
A0A1V6IKH4_9DELT
320
0
36351
TrEMBL
-
A0A6N4CW94_AERSA
607
0
64837
TrEMBL
-
A0A1D8S5E1_9EURY
339
0
36592
TrEMBL
-
A0A1J1AC36_9EURY
308
0
33586
TrEMBL
-
A0A5H7G3U9_SALET
586
0
63347
TrEMBL
-
B3EK06_CHLPB
Chlorobium phaeobacteroides (strain BS1)
402
0
45645
TrEMBL
-
A0A0K2AVT7_STRA7
Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL B-2516)
481
0
51073
TrEMBL
-
Q3B507_CHLL3
Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530)
314
0
34717
TrEMBL
-
A0A4Z0YBZ9_9FIRM
578
0
62519
TrEMBL
-
A0A2N2UAK9_9PROT
603
0
63221
TrEMBL
-
A0A3B1DCT9_9ZZZZ
510
0
57149
TrEMBL
other Location (Reliability: 1)
Q1QB75_PSYCK
Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5)
338
0
37440
TrEMBL
-
A0A1N6BA50_9MYCO
373
0
40387
TrEMBL
-
A0A1E4QBG7_MICAE
613
0
69328
TrEMBL
-
A0A402DHG8_MICAE
633
0
71632
TrEMBL
-
E1RCN9_SEDSS
Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228)
293
0
33375
TrEMBL
-
A1WZ45_HALHL
Halorhodospira halophila (strain DSM 244 / SL1)
311
0
34440
TrEMBL
-
A0A517P040_9BACT
605
0
64527
TrEMBL
-
A0A645DWM1_9ZZZZ
284
0
32131
TrEMBL
other Location (Reliability: 4)
B3EGK6_CHLL2
Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330)
433
0
49387
TrEMBL
-
A0A7R9N6T1_9EURY
97
0
10642
TrEMBL
-
F0VI08_NEOCL
Neospora caninum (strain Liverpool)
333
0
36561
TrEMBL
other Location (Reliability: 1)
E6SKW0_THEM7
Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a)
343
0
38526
TrEMBL
-
A0A132MLH2_9ACTN
382
0
41513
TrEMBL
-
A0A5X5WLN2_SALET
586
0
63185
TrEMBL
-
A0KJ10_AERHH
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049)
599
0
63842
TrEMBL
-
G4T2A2_META2
Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z)
584
0
63567
TrEMBL
-
A0A0A1VZW3_MICAE
613
0
69356
TrEMBL
-
Q1MAP0_RHIL3
Rhizobium leguminosarum bv. viciae (strain 3841)
588
0
63401
TrEMBL
-
K0JXJ8_SACES
Saccharothrix espanaensis (strain ATCC 51144 / DSM 44229 / JCM 9112 / NBRC 15066 / NRRL 15764)
396
0
41610
TrEMBL
-
A0A1L7F5K7_9PSEU
297
0
32256
TrEMBL
-
A0A1V4WWN2_9DELT
314
0
35454
TrEMBL
-
A0A1D7QY31_9BACI
Salisediminibacterium beveridgei
587
0
63945
TrEMBL
-
C7BK46_PHOAA
Photorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77)
583
0
64243
TrEMBL
-
A0A5I5SW49_SALET
586
0
63240
TrEMBL
-
A0A5J6VW15_9PROT
588
0
63007
TrEMBL
-
Q2JHI7_SYNJB
Synechococcus sp. (strain JA-2-3B'a(2-13))
392
0
44006
TrEMBL
-
A0A1F4G886_9BURK
584
0
61975
TrEMBL
-
A0A0W8F6W5_9ZZZZ
300
0
33402
TrEMBL
other Location (Reliability: 3)
C3PK99_CORA7
Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 / CN-1)
324
0
35452
TrEMBL
-
A0A1V6IAC5_9DELT
331
0
38167
TrEMBL
-
F8D4F8_HALXS
Halopiger xanaduensis (strain DSM 18323 / JCM 14033 / SH-6)
417
0
44592
TrEMBL
-
Q08MV0_STIAD
Stigmatella aurantiaca (strain DW4/3-1)
282
0
29822
TrEMBL
-
B3ENK9_CHLPB
Chlorobium phaeobacteroides (strain BS1)
384
0
43067
TrEMBL
-
A0A737RPW8_SALET
586
0
63142
TrEMBL
-
Q6M0V5_METMP
Methanococcus maripaludis (strain S2 / LL)
345
0
38769
TrEMBL
-
A0A0D8FV08_9ACTN
361
0
39737
TrEMBL
-
A0A3B0TRS0_9ZZZZ
603
0
66593
TrEMBL
other Location (Reliability: 3)
B8G132_DESHD
Desulfitobacterium hafniense (strain DSM 10664 / DCB-2)
578
0
63676
TrEMBL
-
A0A1V4XIA3_9DELT
386
0
44083
TrEMBL
-
A0A5Y1WJL5_SALER
586
0
63033
TrEMBL
-
E1R3V2_SEDSS
Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228)
309
0
35406
TrEMBL
-
A4SCZ1_CHLPM
Chlorobium phaeovibrioides (strain DSM 265 / 1930)
399
0
45085
TrEMBL
-
A0A1V5CMH8_9DELT
307
0
35203
TrEMBL
-
A0A2M8B0V0_9DELT
622
0
67047
TrEMBL
-
A0A0H3CU44_ENTCC
Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56)
585
0
63343
TrEMBL
-
A0A1U7MEF3_9FIRM
578
0
63100
TrEMBL
-
D3H0U0_ECO44
Escherichia coli O44:H18 (strain 042 / EAEC)
583
0
63613
TrEMBL
-
A0A644XBI7_9ZZZZ
579
0
63687
TrEMBL
other Location (Reliability: 1)
A0A2H0J1F9_9BURK
593
0
63123
TrEMBL
-
A0A7R9N6P9_9EURY
310
0
34728
TrEMBL
-
A0A5H7JZS7_SALET
586
0
63256
TrEMBL
-
D2RYB9_HALTV
Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 / 4k)
324
0
36188
TrEMBL
-
A0A6J4R5P0_9ACTN
390
0
43128
TrEMBL
-
B8G7U9_CHLAD
Chloroflexus aggregans (strain MD-66 / DSM 9485)
407
0
45376
TrEMBL
-
B9STW8_RICCO
438
0
48253
TrEMBL
Mitochondrion (Reliability: 2)
A0A0E1CSM1_KLEPN
591
0
64024
TrEMBL
-
A0A2N2GIF8_9DELT
620
0
69219
TrEMBL
-
A0A1V5CZZ3_9DELT
318
0
35688
TrEMBL
-
E6PNE9_9ZZZZ
592
0
63540
TrEMBL
other Location (Reliability: 3)
A0A5A5R0C2_MICAE
633
0
71697
TrEMBL
-
A0A5A5RM53_MICAE
395
0
44566
TrEMBL
-
A0A1V6KCP6_9SPIR
310
0
34939
TrEMBL
-
A0A1W9KG29_9PROT
589
0
63605
TrEMBL
-
Q5V5P0_HALMA
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
217
0
24189
TrEMBL
-
A0A5E6M6G5_9BACT
68
0
7520
TrEMBL
-
A0A1F4MTI0_9BURK
596
0
63922
TrEMBL
-
A0A5A5S167_MICAE
395
0
44538
TrEMBL
-
A0A5A5RUS6_MICAE
358
0
38841
TrEMBL
-
A0A1F4D8E2_9PROT
593
0
63511
TrEMBL
-
A0A2M7EPS3_9RHOB
583
0
61346
TrEMBL
-
Q1AWF0_RUBXD
Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1)
394
0
44001
TrEMBL
-
Q3B6S1_CHLL3
Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530)
406
0
45765
TrEMBL
-
A0A6J4LM26_9ACTN
394
0
42539
TrEMBL
-
A0A1M8F6W2_9MYCO
373
0
40401
TrEMBL
-
A0A602W4C2_SALET
583
0
63433
TrEMBL
-
A0A377YTD6_KLEPN
182
0
19943
TrEMBL
-
A0A6W0EQN4_SALET
583
0
63364
TrEMBL
-
M2XZS1_GALSU
481
0
54441
TrEMBL
Secretory Pathway (Reliability: 4)
A0A1F4H9D9_9BURK
589
0
61975
TrEMBL
-
A0A2E7TAC0_9GAMM
586
0
63837
TrEMBL
-
A0A1V4X3D1_9DELT
314
0
35265
TrEMBL
-
A0A0H3CVU9_ENTCC
Enterobacter cloacae subsp. cloacae (strain ATCC 13047 / DSM 30054 / NBRC 13535 / NCTC 10005 / WDCM 00083 / NCDC 279-56)
583
0
63521
TrEMBL
-
Q3MH41_TRIV2
Trichormus variabilis (strain ATCC 29413 / PCC 7937)
635
0
71367
TrEMBL
-
K5BE61_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
376
0
40648
TrEMBL
-
A0A3G3DYM3_SALET
586
0
63183
TrEMBL
-
A0A5J0IDX3_SALET
586
0
63395
TrEMBL
-
A0A606RBK0_SALET
586
0
63411
TrEMBL
-
A0A0K3BEP0_9PSEU
375
0
40033
TrEMBL
-
A0A6J4SM80_9ACTN
402
0
43859
TrEMBL
-
A0A6J4SQ30_9ACTN
311
0
33572
TrEMBL
-
D7CVB5_TRURR
Truepera radiovictrix (strain DSM 17093 / CIP 108686 / LMG 22925 / RQ-24)
326
0
35955
TrEMBL
-
A0A1V4TSK5_9ARCH
306
0
34422
TrEMBL
-
I2B5Q6_SHIBC
Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74)
583
0
62924
TrEMBL
-
A0A7R6R627_9RHOO
584
0
61911
TrEMBL
-
A0A2G9XSD3_9DELT
576
0
60858
TrEMBL
-
F0S488_DESTD
Desulfurobacterium thermolithotrophum (strain DSM 11699 / BSA)
300
0
34239
TrEMBL
-
A0A2P9IMV0_9ACTN
406
0
43276
TrEMBL
-
G4RMF8_THETK
Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)
325
1
37077
TrEMBL
-
A0A1V4WX03_9DELT
326
1
36791
TrEMBL
-
A0A2P6SJB7_ROSCH
412
0
44649
TrEMBL
Chloroplast (Reliability: 2)
A0A829QY74_9GAMM
583
0
63313
TrEMBL
-
K8WSR4_9GAMM
585
0
63670
TrEMBL
-
B4S381_PROA2
Prosthecochloris aestuarii (strain DSM 271 / SK 413)
404
0
45519
TrEMBL
-
D9S045_THEOJ
Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 / JW/IW-1228P)
295
0
33644
TrEMBL
-
A0A6J4SMY8_9ACTN
373
0
40175
TrEMBL
-
F2RI92_STRVP
Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745)
376
0
40398
TrEMBL
-
A0A6C6ZAC5_SALPB
583
0
63549
TrEMBL
-
A0A654AK39_9GAMM
586
0
63383
TrEMBL
-
B2T6S3_PARPJ
Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
584
0
62819
TrEMBL
-
F6BC39_METIK
Methanotorris igneus (strain DSM 5666 / JCM 11834 / Kol 5)
335
0
37900
TrEMBL
-
A0A517SUV1_9BACT
590
0
62861
TrEMBL
-
F6D7P2_METPW
Methanobacterium paludis (strain DSM 25820 / JCM 18151 / SWAN1)
332
0
37396
TrEMBL
-
Q0VPZ9_ALCBS
Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
348
0
38075
TrEMBL
-
A0A1E4GUV3_9CAUL
587
0
62888
TrEMBL
-
A0A0B6TYG6_9CORY
319
0
34942
TrEMBL
-
A0A3B1D5A3_9ZZZZ
510
0
57129
TrEMBL
other Location (Reliability: 1)
M5CHD7_THACB
Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14)
487
2
53328
TrEMBL
other Location (Reliability: 1)
A0A166EBX3_9EURY
335
0
37097
TrEMBL
-
A0A1N6B9T1_9MYCO
315
0
33331
TrEMBL
-
F1TD39_9FIRM
391
0
45175
TrEMBL
-
A0A1U3U8Y8_9MYCO
423
0
45372
TrEMBL
-
A6UVR0_META3
Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)
341
0
38435
TrEMBL
-
B3QRC1_CHLP8
Chlorobaculum parvum (strain DSM 263 / NCIMB 8327)
401
0
45617
TrEMBL
-
A0A2U3LTQ4_9BACT
395
0
44529
TrEMBL
-
A0A0A8X684_9BACI
590
0
65518
TrEMBL
-
A9KRJ6_LACP7
Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
385
0
43692
TrEMBL
-
A0A7Y8KYE5_9BURK
603
0
63589
TrEMBL
-
C7P537_HALMD
Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541)
643
0
70572
TrEMBL
-
B3QTL2_CHLT3
Chloroherpeton thalassium (strain ATCC 35110 / GB-78)
383
0
43229
TrEMBL
-
A0A644UMB6_9ZZZZ
570
0
62505
TrEMBL
other Location (Reliability: 1)
A0A644Y272_9ZZZZ
580
0
63680
TrEMBL
other Location (Reliability: 2)
A0A645CPC0_9ZZZZ
177
0
19866
TrEMBL
other Location (Reliability: 1)
ASNA_CAEEL
342
0
37554
Swiss-Prot
other Location (Reliability: 2)
GET3_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
354
0
39354
Swiss-Prot
-
ARSA_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
349
0
39919
Swiss-Prot
-
ARSA_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
324
0
36544
Swiss-Prot
-
GET3_ASPFU
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
340
0
37440
Swiss-Prot
other Location (Reliability: 4)
GET3_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
329
0
36548
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63000
63000
x * 63000, ArsA, containing two ABC domains, structure model, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
the enzyme is composed of ATPase subunit ArsA and arsenic-efflux pump ArsB
additional information
?
x * 63000, ArsA, containing two ABC domains, structure model, overview
additional information
-
the ArsA protein is a membrane associated ATPase, energizing the arsenite efflux pump by ATP hydrolysis, ArsA is attached to the ArsB inner-membrane protein. The ArsB protein can function alone as a chemiosmotic, membrane-potential driven arsenite-efflux transporter or together with ArsA as an ATP-driven primary membrane pump. ArsC reduces loss toxic arsenate to more toxic arsenite, the substrate for the ArsB transport protein
additional information
-
the ArsA is a 63000 Da protein, Ars B is a 45500 Da protein, ArsC is a 16000 Da, protein. ArsB, with 12 membrane-spanning segments forms the channel part and ArsA, occuring in pairs peripherally to the membrane
additional information
ArsA ATPase, the catalytic subunit of the pump, has two homologous halves, A1 and A2, and at the interface of these two halves are two nucleotide-binding domains and a metalloid-binding domain, Cys113 and Cys422 form a high-affinity metalloid binding site. There is only a single high-affinity metalloid binding site in ArsA, and second that Cys172 controls the affinity of this site for metalloid and hence the efficiency of metalloactivation of the ArsAB efflux pump
additional information
-
ArsA is composed of two homologous halves A1 and A2, each containing a nucleotide binding domain, and a single metalloid binding or activation domain is located at the interface of the two halves of the protein. The metalloid binding domain is connected to the two nucleotide binding domains through two DTAPTGH sequences, one in A1 and the other in A2. The DTAPTGH sequences are proposed to be involved in information communication between the metal and catalytic sites
additional information
-
ArsA is the catalytic subunit of the ArsAB arsenite (As(III)) translocating ATPase, ArsA exhibits ATpase activity
additional information
-
ArsA structure analysis and comparison, PDB entry 1F48, overview
additional information
-
subunit ArsA exhibuts ATPase activity and subunit ArsB is a 12 alpha-helix transmembrane spanning pump extruding As(III) and Sb(III)
additional information
-
ArsA structure analysis and comparison, PDB entry 1F48, overview
-
additional information
-
the Strop634-Strop1447 protein interface is compatible permitting heterotetramer formation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic subunit of the ATP-dependent arsenite pump is encoded by the Escherichia coli plasmid R773
-
hanging drop vapour diffusion method at 30°C, space group P21212 when AATP or AMP-PMP is bound, space group I222 in presence of ADP * A1F3
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C108A
-
alteration of either Cys108 or Cys120 to alanine results in loss of metalloid binding to either pre-mixed or copurified AmArsAs, indicating that the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain
C120A
-
alteration of either Cys108 or Cys120 to alanine results in loss of metalloid binding to either pre-mixed or copurified AmArsAs, indicating that the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain
C113A/C422A
C172A
site-directed mutagenesis, an ArsA mutant, the mutant shows reduced affinity for Sb(III) compared to the wild-type enzyme
C172A/H453A
site-directed mutagenesis, the ArsA double mutant exhibits significantly decreased affinity for Sb(III)
D142A
-
site-directed mutagenesis, the mutant is activated by arsenite and antimonite in a similar amount as the wild-type enzyme
D142E
-
site-directed mutagenesis, the mutant is stronger activated by arsenite and antimonite compared to the wild-type enzyme
D142N
-
site-directed mutagenesis, the mutant is activated by arsenite and antimonite in a similar amount as the wild-type enzyme
D447A
-
site-directed mutagenesis, the mutant is less activated by arsenite and antimonite compared to the wild-type enzyme
D447E
-
site-directed mutagenesis, the mutant is less activated by arsenite and antimonite compared to the wild-type enzyme
D447N
-
site-directed mutagenesis, the near complete insolubility of D447N ArsA precludes its purification and biochemical characterization
D45A
-
mutant of ArsA, the catalytic subunit of the pump. Inactive enzyme. ATP and Sb(III) synergistically protect wild type ArsA catalytic subunit from trypsin digestion. Subsequent addition of Mg2+ increases trypsin digestion. Mutant D45N and D45A remain protected by ATP and Sb(III) but lose the Mg2+ effect
D45E
-
approximately 5% of the wild type activity with about a 5fold decrease in affinity for Mg2+. ATP and Sb(III) synergistically protect wild type ArsA catalytic subunit from trypsin digestion. Subsequent addition of Mg2+ increases trypsin digestion, D45E exhibits an lower Mg2+ response
D45N
-
mutant of Ars A, the catalytic subunit of the pump. Inactive enzyme. ATP and Sb(III) synergistically protect wild type ArsA catalytic subunit from trypsin digestion. Subsequent addition of Mg2+ increases trypsin digestion. Mutant D45N and D45A remain protected by ATP and Sb(III) but lose the Mg2+ effect
DELTA1-277
-
same arsenite resistance like wild-type when coexpressed with DELTA280-583 or DELTA324-583
DELTA1-320
-
no arsenite resistance in cells expressing that protein in combination with DELTA280-583 but resistance like wild-type expressing cells when expressed in combination with DELTA324-583
DELTA280-583
-
no arsenite resistance in cells expressing that protein in combination with DELTA1-320 but resistance like wild-type expressing cells when expressed in combination with DELTA1-277
DELTA324-583
-
same arsenite resistance like wild-type when coexpressed with DELTA1-320 or DELTA1-277
G18D
-
mutation in ArsA protein, loss of resistance to the toxic oxyanions as well as inability to extrude arsenite
G18R
-
mutation in ArsA protein, loss of resistance to the toxic oxyanions as well as inability to extrude arsenite
G18S
-
loss of resistance towards arsenite and no nucleotide-binding in A1 NBD
G20S
-
mutation in ArsA protein, loss of resistance to the toxic oxyanions as well as inability to extrude arsenite
G337R
H138A
-
cells with this protein were resistant to arsenite and antimonite like wild-type
H148A
-
cells with this protein were resistant to arsenite and antimonite like wild-type, 3-fold lowering of the antimonite stimulated ATPase activity compared to wild-type enzyme
H148A/S420A
site-directed mutagenesis, the mutant exhibits a half-maximal stimulation similar to that of the wild-type enzyme
H219A
-
cells with this protein were resistant to arsenite and antimonite like wild-type
H327A
-
cells with this protein were resistant to arsenite and antimonite like wild-type
H359A
-
cells with this protein were resistant to arsenite and antimonite like wild-type
H368A
-
cells with this protein were resistant to arsenite and antimonite like wild-type, 3-fold lowering of the antimonite stimulated ATPase activity compared to wild-type enzyme
H388A
-
cells with this protein were resistant to arsenite and antimonite like wild-type
H397A
-
cells with this protein were resistant to arsenite and antimonite like wild-type
H453A
-
cells with this protein were resistant to arsenite and antimonite like wild-type, 3-fold lowering of the antimonite stimulated ATPase activity compared to wild-type enzyme
H465A
-
cells with this protein were resistant to arsenite and antimonite like wild-type
H477A
-
cells with this protein were resistant to arsenite and antimonite like wild-type
H520A
-
cells with this protein were resistant to arsenite and antimonite like wild-type
H558A
-
cells with this protein were resistant to arsenite and antimonite like wild-type, 50% lowering of the antimonite stimulated ATPase activity compared to wild-type enzyme
K16Q
-
site-directed mutagenesis, the mutant ArsA shows 70% of wild-type ATPase activity
K335Q
-
site-directed mutagenesis, the mutant ArsA is inactive. K335Q acquires a closed conformation during metalloid-stimulated catalysis that is different from the open conformation of the wild-type
K340E
-
retains about 10% of wild-type ATPase activity, no antimonite-stimulated ATPase activity
M446W
-
no changes in resistance towards arsenite or in specific activity compared to wild-type
Q56R
-
the mutant exhibits significant metalloid-stimulated ATPase activity in vitro
T22I
-
mutation in ArsA protein, loss of resistance to the toxic oxyanions as well as inability to extrude arsenite
K16Q
-
site-directed mutagenesis, the mutant ArsA shows 70% of wild-type ATPase activity
-
K335Q
-
site-directed mutagenesis, the mutant ArsA is inactive. K335Q acquires a closed conformation during metalloid-stimulated catalysis that is different from the open conformation of the wild-type
-
C113A/C422A
-
mutant ArsA has basal ATPase activity similar to that of the wild type but lacks metalloid-stimulated activity
-
additional information
C113A/C422A
-
mutant ArsA has basal ATPase activity similar to that of the wild type but lacks metalloid-stimulated activity
C113A/C422A
site-directed mutagenesis, the mutant lacks As(III) activation activity compared to the wild-type enzyme
G337R
-
mutation in ArsA protein, complete loss of resistance to the toxic oxyanions
G337R
-
loss of resistance towards arsenite and no nucleotide-binding in A2 NBD
additional information
-
heterologous expression of one of the Alkaliphilus metalliredigens ars operons (ars1) confers arsenite but not antimonite resistance to DELTAars Escherichia coli strain AW3110. Only the co-expressed AmArsA1 and AmArsA2 display arsenite or antimonite stimulate ATPase activity, phenotype, overview
additional information
asna-1-mutant nematodes are more sensitive to As(III) and Sb(III) toxicity than are wild-type animals
additional information
-
asna-1-mutant nematodes are more sensitive to As(III) and Sb(III) toxicity than are wild-type animals
additional information
construction of a chimeric mutant fusion enzyme NifH-ArsA consisting of subunits from ArsA and NifH a component of the nitrogenase enzyme complex, the mutant chimeric NifH-ArsA2 can substitute for the ArsA in arsenic reduction, overview
additional information
T-289 clones with siRNA decreased ASNA1 expression exhibit 51% longer doubling times than wild-type T-289 cells. After exposure to cisplatin, ASNA1 downregulated cells display a significant increase in apoptosis. The cisplatin IC50 in ASNA1 underexpressing cells is 41.7% of the IC50 for wild-type cells, and the arsenite IC50 is 59.9% of wild-type IC50. Phenotypes, overview
additional information
-
T-289 clones with siRNA decreased ASNA1 expression exhibit 51% longer doubling times than wild-type T-289 cells. After exposure to cisplatin, ASNA1 downregulated cells display a significant increase in apoptosis. The cisplatin IC50 in ASNA1 underexpressing cells is 41.7% of the IC50 for wild-type cells, and the arsenite IC50 is 59.9% of wild-type IC50. Phenotypes, overview
additional information
-
construction of a truncated mutant by gene deletions disrupting strop634 and strop1447 in strain CNB-440, lack of Strop634 renders the single and double deletion strains highly sensitive to arsenate exposure, whereas in the absence of Strop1447, the cells unexpectedly display a normal resistance level, complementation of ACR2 deficient yeast strains by expression of Strop634, overview
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ATP and Sb(III) synergistically protect wild type ArsA catalytic subunit from trypsin digestion. Subsequent addition of Mg2+ increases trypsin digestion. Mutant D45N and D45A remain protected by ATP and Sb(III) but lose the Mg2+ effect. D45E exhibits an intermediate Mg2+ response
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes by nickel affinity chromatography
-
recombinant His6-tagged wild-type and mutant ArsA from Escherichia coli strain JM109 to over 95% homogeneity by nickel affinity chromatography
-
recombinant maltose-binding-protein fusion protein from Escherichia coli by amylose affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of ArsA and ArsD wild-type and mutants in a Saccharomyces cerevisiae two-hybrid system
-
expression of ArsA and ArsD wild-type and mutants in a Saccharomyces cerevisiae two-hybrid system for interaction analysis, overview
-
expression of His6-tagged wild-type and mutant ArsA in Escherichia coli strain JM109. At high expression level wild-type ArsA is located in the cytosol, mutants D142A, D142E, and D142N are also found predominantly in the cytosol at similar levels as the wild type, but D447A and D447E proteins are found as insoluble aggregates, while only trace amounts of D447N can be observed in the soluble fraction
-
expression of the enzyme as maltose-binding-protein fusion protein in Escherichia coli
gene arsA, expression of isolated ArsA ATPase in Escherichia coli strain BL21 (DE3)
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gene arsA, phylogenetic analysis with detailed analysis of clustering in the superfamily, overview
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gene arsA, phylogenetic analysis, expression of complete ArsA, partial ArsA2, or chimeric NifH-ArsA2 in Escherichia coli strain JM109, BG1754 (arsAB), BG1757 (arsA2B), and BG1791 (nifH-arsA2B)
gene arsB, DNA and amino acid sequence determination and analysis, phylogenetic analysis
genes strop634 and strop1447, expression of enzyme mutants in Escherichia coli strain EPI300 with pCC1FOS-based fosmids
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the ars operon of the plasmid R773 contains a regulatory gene, arsR, and three structural genes, arsA, arsB, and arsC
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the arsenical resistance operon from IncN plasmid R46 contains the five genes ArsR, arsD, arsA, arsB and arsC. The chromosomal ars operon contains only arsB, arsC, and arsR
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transfection of T-289 melanoma cells with either ASNA1 sense or ASNA1 antisense constructs, expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is induced by arsenate (but not phosphate) with maximum induction 4-6xa0h after addition of 0.35xa0mM arsenate
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhou, T.; Rosen, B.P.; Gatti, D.L.
Crystallization and preliminary X-ray analysis of the catalytic subunit of the ATP-dependent arsenite pump encoded by the Escherichia coli plasmid R773
Acta Crystallogr. Sect. D
55
921-924
1999
Escherichia coli
Rosen, B.P.; Weigel, U.; Monticello, R.A.; Edwards, B.P.F.
Molecular analysis of an anion pump: purification of the ArsC protein
Arch. Biochem. Biophys.
284
381-385
1991
Escherichia coli
Rosen, B.P.; Bhattacharjee, H.; Shi, W.
Mechanism of metalloregulation of an anion-translocating ATPase
J. Bioenerg. Biomembr.
27
85-91
1995
Escherichia coli
Zhou, T.; Rosen, B.P.
Asp45 is a Mg2+ ligand in the ArsA ATPase
J. Biol. Chem.
274
13854-13858
1999
Escherichia coli
Zhou, T.; Rosen, B.P.
Tryptophan fluorescence reports nucleotide-induced conformational changes in a domain of the ArsA ATPase
J. Biol. Chem.
272
19731-19737
1997
Escherichia coli
Bruhn, D.F.; Li, J.; Silver, S.; Roberto, F.; Rosen, B.P.
The arsenical resistance operon of IncN plasmid R46
FEMS Microbiol. Lett.
139
149-153
1996
Escherichia coli
Silver, S.
Bacterial resistance to toxic metal ions - a review
Gene
179
9-19
1996
Escherichia coli, Staphylococcus aureus, Staphylococcus carnosus
Owolabi, J.B.; Rosen, B.P.
Differential mRNA stability controls relative gene expression within the plasmid-encoded arsenical resistance operon
J. Bacteriol.
172
2367-2371
1990
Escherichia coli
Dey, S.; Dou, D.; Rosen, B.P.
ATP-dependent arsenite transport in everted membrane vesicles of Escherichia coli
J. Biol. Chem.
269
25442-25446
1994
Escherichia coli
Kaur, P.; Rosen, B.P.
Plasmid-encoded resistance to arsenite and antimon
Plasmid
27
29-40
1992
Escherichia coli, Staphylococcus aureus, Staphylococcus xylosus
Walmsley, A.R.; Zhou, T.; Borges-Walmsley, M.I.; Rosen, B.P.
Antimonite regulation of the ATPase activity of ArsA, the catalytic subunit of the arsenical pump
Biochem. J.
360
589-597
2001
Escherichia coli
Bhattacharjee, H.; Rosen, B.P.
Structure-function analysis of the ArsA ATPase: contribution of histidine residues
J. Bioenerg. Biomembr.
33
459-468
2001
Escherichia coli
Jia, H.; Kaur, P.
Role of the linker region of the anion-stimulated ATPase ArsA. Effect of deletion and point mutations in the linker region
J. Biol. Chem.
276
29582-29587
2001
Escherichia coli
Zhou, T.; Radaev, S.; Rosen, B.P.; Gatti, D.L.
Conformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation
J. Biol. Chem.
276
30414-30422
2001
Escherichia coli
Zhou, T.; Shen, J.; Liu, Y.; Rosen, B.P.
Unisite and multisite catalysis in the ArsA ATPase
J. Biol. Chem.
277
23815-23820
2002
Escherichia coli
Ruan, X.; Bhattacharjee, H.; Rosen, B.P.
Cys-113 and Cys-422 form a high affinity metalloid binding site in the ArsA ATPase
J. Biol. Chem.
281
9925-9934
2006
Escherichia coli, Escherichia coli plasmid R773
Tseng, Y.Y.; Yu, C.W.; Liao, V.H.
Caenorhabditis elegans expresses a functional ArsA
FEBS J.
274
2566-2572
2007
Caenorhabditis elegans (P30632), Caenorhabditis elegans
Lin, Y.F.; Yang, J.; Rosen, B.P.
ArsD: an As(III) metallochaperone for the ArsAB As(III)-translocating ATPase
J. Bioenerg. Biomembr.
39
453-458
2007
Escherichia coli
Lin, Y.F.; Yang, J.; Rosen, B.P.
ArsD residues Cys12, Cys13, and Cys18 form an As(III)-binding site required for arsenic metallochaperone activity
J. Biol. Chem.
282
16783-16791
2007
Escherichia coli
Ruan, X.; Bhattacharjee, H.; Rosen, B.P.
Characterization of the metalloactivation domain of an arsenite/antimonite resistance pump
Mol. Microbiol.
67
392-402
2008
Escherichia coli (P08690)
Lin, Y.F.; Walmsley, A.R.; Rosen, B.P.
An arsenic metallochaperone for an arsenic detoxification pump
Proc. Natl. Acad. Sci. USA
103
15617-15622
2006
Escherichia coli
Lahiri, S.; Pulakat, L.; Gavini, N.
Functional participation of a nifH-arsA2 chimeric fusion gene in arsenic reduction by Escherichia coli
Biochem. Biophys. Res. Commun.
368
311-317
2008
Escherichia coli (P08690)
Bhattacharjee, H.; Choudhury, R.; Rosen, B.P.
Role of conserved aspartates in the ArsA ATPase
Biochemistry
47
7218-7227
2008
Escherichia coli
Hemmingsson, O.; Zhang, Y.; Still, M.; Naredi, P.
ASNA1, an ATPase targeting tail-anchored proteins, regulates melanoma cell growth and sensitivity to cisplatin and arsenite
Cancer Chemother. Pharmacol.
63
491-499
2009
Homo sapiens (O43681), Homo sapiens
Chang, J.S.; Ren, X.; Kim, K.W.
Biogeochemical cyclic activity of bacterial arsB in arsenic-contaminated mines
J. Environ. Sci. (China)
20
1348-1355
2008
Pseudomonas putida (Q2VA10), Pseudomonas putida (Q2VBP9), Pseudomonas putida (Q38J49), Pseudomonas putida
Wu, B.; Song, J.; Beitz, E.
Novel channel enzyme fusion proteins confer arsenate resistance
J. Biol. Chem.
285
40081-40087
2010
Frankia alni, Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Salinispora tropica
Fu, H.; Ajees, A.; Rosen, B.; Bhattacharjee, H.
Role of signature lysines in the deviant walker a motifs of the ArsA ATPase
Biochemistry
49
356-364
2010
Escherichia coli, Escherichia coli JM109
Yang, J.; Rawat, S.; Stemmler, T.L.; Rosen, B.P.
Arsenic binding and transfer by the ArsD As(III) metallochaperone
Biochemistry
49
3658-3666
2010
Escherichia coli
Ye, J.; Ajees, A.A.; Yang, J.; Rosen, B.P.
The 1.4 A crystal structure of the ArsD arsenic metallochaperone provides insights into its interaction with the ArsA ATPase
Biochemistry
49
5206-5212
2010
Saccharomyces cerevisiae
Ajees, A.A.; Yang, J.; Rosen, B.P.
The ArsD As(III) metallochaperone
Biometals
24
391-399
2011
Escherichia coli
Liu, C.; Balsamo, V.; Sun, D.; Naja, M.; Wang, X.; Rosen, B.; Li, C.Z.
A 3D localized surface plasmon resonance biosensor for the study of trivalent arsenic binding to the ArsA ATPase
Biosens. Bioelectron.
38
19-26
2012
Escherichia coli
Fu, H.L.; Rosen, B.P.; Bhattacharjee, H.
Biochemical characterization of a novel ArsA ATPase complex from Alkaliphilus metalliredigens QYMF
FEBS Lett.
584
3089-3094
2010
Alkaliphilus metalliredigens
Castillo, R.; Saier, M.H.
Functional promiscuity of homologues of the bacterial ArsA ATPases
Int. J. Microbiol.
2010
187373
2010
Escherichia coli
Pillai, J.K.; Venkadesh, S.; Ajees, A.A.; Rosen, B.P.; Bhattacharjee, H.
Mutations in the ArsA ATPase that restore interaction with the ArsD metallochaperone
Biometals
27
1263-1275
2014
Escherichia coli
Sri Lakshmi Sunita, M.; Prashant, S.; Bramha Chari, P.; Nageswara Rao, S.; Balaravi, P.; Kavi Kishor, P.
Molecular identification of arsenic-resistant estuarine bacteria and characterization of their ars genotype
Ecotoxicology
21
202-212
2012
uncultured bacterium
Maldonado-Mendoza, I.; Harrison, M.
RiArsB and RiMT-11 Two novel genes induced by arsenate in arbuscular mycorrhiza
Fungal Biol.
122
121-130
2018
Rhizophagus irregularis
Shilpa, T.; Rosen, B.; Ajees, A.
Structural studies of the ArsD arsenic metallochaperone using molecular dynamics
J. Comput. Methods Sci. Eng.
17
227-233
2017
Escherichia coli (P08690 and P0AB93)
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EXTERNAL LINKS (specific for EC-Number 7.3.2.7)
Transporter Classification Database (TCDB): 3.A.4.1.1, 3.A.19.1.3
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