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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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Word Map
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACR3
ACR3-ArsC
ACR3-ArsC fusion protein
ARSA
ArsA ATPase
ArsAB
ArsAB pump
Arsenical resistance ATPase
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-
-
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Arsenite-translocating ATPase
Arsenite-transporting ATPase
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-
-
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ATP-dependent arsenite pump
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EC 3.6.3.16
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formerly
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RiArsB
-
arsenate/arsenite permease component of ArsAB arsenite efflux pump
Rv2643
ARSA
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-
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ArsA ATPase
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Arsenite-translocating ATPase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + arsenite[side 1] = ADP + phosphate + arsenite[side 2]
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
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-
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PATHWAY SOURCE
PATHWAYS
-
, , ,
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + 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
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?
ATP + H2O + antimonite/in
ADP + phosphate + antimonite/out
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-
-
-
?
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
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-
?
ATP + H2O + antimonite/in
ADP + phosphate + antimonite/out
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-
-
-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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-
-
-
?
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
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?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
the ars operon confers resistance to arsenite, arsenate and antimonite
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?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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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
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-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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mechanism of transcriptional regulation by the ArssR repressor and allosteric regulation of the ArsA protein, the catalytic subunit of the pump
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-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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detoxifying system
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-
?
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
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-
?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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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
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-
?
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
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-
?
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
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?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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ArsA ATPase is the catalytic subunit of the ArsAB pump
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?
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
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?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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metalloid-binding site MBS1 is involved in metalloid transfer and ArsA activation
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?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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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
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?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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binding of As(III) to ArsA is greatly facilitated by the presence of magnesium ion and ATP
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?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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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
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?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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?
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
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?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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the ars operon confers resistance to arsenite, arsenate and antimonite
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?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
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?
ATP + H2O + arsenite/in
ADP + phosphate + arsenite/out
-
the ars operon confers resistance to arsenite, arsenate and antimonite
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-
?
ATP + H2O + arsenite[side 1]
ADP + phosphate + arsenite[side 2]
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-
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?
additional information
?
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the AmArsA1-AmArsA2 complex has metalloid-stimulated ATPase activity. ArsB transports antimonite, while Acr3 does not appear to do so
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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ArsA specifically interacts with ArsD but not with ArsR or ArsC
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?
additional information
?
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the mutant chimeric NifH-ArsA2 can substitute for the ArsA in arsenic reduction, overview
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?
additional information
?
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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
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?
additional information
?
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ArsA is the catalytic subunit of the ArsAB arsenite (As(III)) translocating ATPase, ArsA exhibits ATpase activity
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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.
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?
additional information
?
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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.
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
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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
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-
-
-
?
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
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detoxifying system
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-
?
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.
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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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
-
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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
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ArsD
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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
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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
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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
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ArsD
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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
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cardiomyopathies
Biallelic Variants in ASNA1, Encoding a Cytosolic Targeting Factor of Tail-Anchored Proteins, Cause Rapidly Progressive Pediatric Cardiomyopathy.
Cardiomyopathies
Correction to: Biallelic Variants in ASNA1, Encoding a Cytosolic Targeting Factor of Tail-Anchored Proteins, Cause Rapidly Progressive Pediatric Cardiomyopathy.
Immune System Diseases
Comparative transcriptome analysis of Eriocheir japonica sinensis response to environmental salinity.
Melanoma
ASNA1, an ATPase targeting tail-anchored proteins, regulates melanoma cell growth and sensitivity to cisplatin and arsenite.
Neoplasms
Depletion of the ER chaperone ENPL-1 sensitizes C. elegans to the anticancer drug cisplatin.
Ovarian Neoplasms
Increased sensitivity to platinating agents and arsenite in human ovarian cancer by downregulation of ASNA1.
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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
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28.87
purified recombinant MBP-fusion enzyme stimulated by 0.5 mM Sb3+
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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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
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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
-
-
brenda
genes strop634 and strop1447 encoding ACR2 and Ars2, respectively
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-
brenda
-
-
-
brenda
gene arsA, encoding for the catalytic subunit of the the ArsAB pump
Uniprot
brenda
gene arsAB in the arsRDABC operon is encoded on intracellular plasmid R773
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brenda
strains JM109 and BL21, ArsA ATPase is the catalytic subunit of the ArsAB pump encoded by the arsRDABC operon of Escherichia coli plasmid R773
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the enzyme is encoded by the ars operon of plasmid R773
Uniprot
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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ArsA protein is an extrinsic membrane protein, ArsB protein is an integral membrane protein
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
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phylogenetic analysis of gene arsA and prokaryotic and eukaryotic ArsA homologues with detailed analysis of clustering in the superfamily, overview
evolution
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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
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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
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malfunction
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mutations rendered the aquaglyceroporin channel more polar resulting in lower glycerol permeability and enhanced arsenite selectivity
malfunction
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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
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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
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physiological function
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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
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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
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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
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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
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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
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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
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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
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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
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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
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physiological function
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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
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additional information
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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
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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
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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
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the Cys108 of AmArsA1 and Cys120 of AmArsA2 form part of the metalloid binding domain
additional information
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the Strop634 channel domain has enhanced selectivity for arsenite and low glycerol permeability
additional information
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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
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Show AA Sequence and Transmembrane Helices (2896 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63000
63000
x * 63000, ArsA, containing two ABC domains, structure model, overview
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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
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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
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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
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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
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ArsA is the catalytic subunit of the ArsAB arsenite (As(III)) translocating ATPase, ArsA exhibits ATpase activity
additional information
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ArsA structure analysis and comparison, PDB entry 1F48, overview
additional information
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subunit ArsA exhibuts ATPase activity and subunit ArsB is a 12 alpha-helix transmembrane spanning pump extruding As(III) and Sb(III)
additional information
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ArsA structure analysis and comparison, PDB entry 1F48, overview
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additional information
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the Strop634-Strop1447 protein interface is compatible permitting heterotetramer formation
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic subunit of the ATP-dependent arsenite pump is encoded by the Escherichia coli plasmid R773
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C108A
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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
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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
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site-directed mutagenesis, the mutant is activated by arsenite and antimonite in a similar amount as the wild-type enzyme
D142E
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site-directed mutagenesis, the mutant is stronger activated by arsenite and antimonite compared to the wild-type enzyme
D142N
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site-directed mutagenesis, the mutant is activated by arsenite and antimonite in a similar amount as the wild-type enzyme
D447A
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site-directed mutagenesis, the mutant is less activated by arsenite and antimonite compared to the wild-type enzyme
D447E
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site-directed mutagenesis, the mutant is less activated by arsenite and antimonite compared to the wild-type enzyme
D447N
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site-directed mutagenesis, the near complete insolubility of D447N ArsA precludes its purification and biochemical characterization
D45A
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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
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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
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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
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same arsenite resistance like wild-type when coexpressed with DELTA280-583 or DELTA324-583
DELTA1-320
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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
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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
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same arsenite resistance like wild-type when coexpressed with DELTA1-320 or DELTA1-277
G18D
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mutation in ArsA protein, loss of resistance to the toxic oxyanions as well as inability to extrude arsenite
G18R
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mutation in ArsA protein, loss of resistance to the toxic oxyanions as well as inability to extrude arsenite
G18S
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loss of resistance towards arsenite and no nucleotide-binding in A1 NBD
G20S
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mutation in ArsA protein, loss of resistance to the toxic oxyanions as well as inability to extrude arsenite
G337R
H138A
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cells with this protein were resistant to arsenite and antimonite like wild-type
H148A
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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
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cells with this protein were resistant to arsenite and antimonite like wild-type
H327A
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cells with this protein were resistant to arsenite and antimonite like wild-type
H359A
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cells with this protein were resistant to arsenite and antimonite like wild-type
H368A
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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
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cells with this protein were resistant to arsenite and antimonite like wild-type
H397A
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cells with this protein were resistant to arsenite and antimonite like wild-type
H453A
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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
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cells with this protein were resistant to arsenite and antimonite like wild-type
H477A
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cells with this protein were resistant to arsenite and antimonite like wild-type
H520A
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cells with this protein were resistant to arsenite and antimonite like wild-type
H558A
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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
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site-directed mutagenesis, the mutant ArsA shows 70% of wild-type ATPase activity
K335Q
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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
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retains about 10% of wild-type ATPase activity, no antimonite-stimulated ATPase activity
M446W
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no changes in resistance towards arsenite or in specific activity compared to wild-type
Q56R
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the mutant exhibits significant metalloid-stimulated ATPase activity in vitro
T22I
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mutation in ArsA protein, loss of resistance to the toxic oxyanions as well as inability to extrude arsenite
K16Q
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site-directed mutagenesis, the mutant ArsA shows 70% of wild-type ATPase activity
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K335Q
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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
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C113A/C422A
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mutant ArsA has basal ATPase activity similar to that of the wild type but lacks metalloid-stimulated activity
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additional information
C113A/C422A
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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
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mutation in ArsA protein, complete loss of resistance to the toxic oxyanions
G337R
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loss of resistance towards arsenite and no nucleotide-binding in A2 NBD
additional information
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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
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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
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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
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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
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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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes by nickel affinity chromatography
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recombinant His6-tagged wild-type and mutant ArsA from Escherichia coli strain JM109 to over 95% homogeneity by nickel affinity chromatography
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recombinant maltose-binding-protein fusion protein from Escherichia coli by amylose affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of ArsA and ArsD wild-type and mutants in a Saccharomyces cerevisiae two-hybrid system
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expression of ArsA and ArsD wild-type and mutants in a Saccharomyces cerevisiae two-hybrid system for interaction analysis, overview
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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
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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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is induced by arsenate (but not phosphate) with maximum induction 4-6xa0h after addition of 0.35xa0mM arsenate
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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
brenda
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
brenda
Rosen, B.P.; Bhattacharjee, H.; Shi, W.
Mechanism of metalloregulation of an anion-translocating ATPase
J. Bioenerg. Biomembr.
27
85-91
1995
Escherichia coli
brenda
Zhou, T.; Rosen, B.P.
Asp45 is a Mg2+ ligand in the ArsA ATPase
J. Biol. Chem.
274
13854-13858
1999
Escherichia coli
brenda
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
brenda
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
brenda
Silver, S.
Bacterial resistance to toxic metal ions - a review
Gene
179
9-19
1996
Escherichia coli, Staphylococcus aureus, Staphylococcus carnosus
brenda
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
brenda
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
brenda
Kaur, P.; Rosen, B.P.
Plasmid-encoded resistance to arsenite and antimon
Plasmid
27
29-40
1992
Escherichia coli, Staphylococcus aureus, Staphylococcus xylosus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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)
brenda
Bhattacharjee, H.; Choudhury, R.; Rosen, B.P.
Role of conserved aspartates in the ArsA ATPase
Biochemistry
47
7218-7227
2008
Escherichia coli
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Ajees, A.A.; Yang, J.; Rosen, B.P.
The ArsD As(III) metallochaperone
Biometals
24
391-399
2011
Escherichia coli
brenda
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
brenda
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
brenda
Castillo, R.; Saier, M.H.
Functional promiscuity of homologues of the bacterial ArsA ATPases
Int. J. Microbiol.
2010
187373
2010
Escherichia coli
brenda
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
brenda
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
brenda
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
brenda
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)
-
brenda
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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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