EC Number | Cloned (Comment) | Organism |
---|---|---|
7.3.2.7 | recombinant expression of His-tagged wild-type and mutant enzymes | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
7.3.2.7 | K16Q | site-directed mutagenesis, the mutant ArsA shows 70% of wild-type ATPase activity | Escherichia coli |
7.3.2.7 | 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 | Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
7.3.2.7 | Mg2+ | required | Escherichia coli | |
7.3.2.7 | 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 | Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
7.3.2.7 | 63000 | - |
x * 63000, recombinant ArsA, SDS-PAGE | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
7.3.2.7 | ATP + H2O + antimonite/in | Escherichia coli | - |
ADP + phosphate + antimonite/out | - |
? | |
7.3.2.7 | ATP + H2O + antimonite/in | Escherichia coli JM109 | - |
ADP + phosphate + antimonite/out | - |
? | |
7.3.2.7 | ATP + H2O + arsenite/in | Escherichia coli | - |
ADP + phosphate + arsenite/out | - |
? | |
7.3.2.7 | ATP + H2O + arsenite/in | Escherichia coli JM109 | - |
ADP + phosphate + arsenite/out | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
7.3.2.7 | Escherichia coli | - |
gene arsA | - |
7.3.2.7 | Escherichia coli JM109 | - |
gene arsA | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
7.3.2.7 | recombinant His-tagged wild-type and mutant enzymes by nickel affinity chromatography | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
7.3.2.7 | ATP + H2O + antimonite/in | - |
Escherichia coli | ADP + phosphate + antimonite/out | - |
? | |
7.3.2.7 | ATP + H2O + antimonite/in | - |
Escherichia coli JM109 | ADP + phosphate + antimonite/out | - |
? | |
7.3.2.7 | ATP + H2O + arsenite/in | - |
Escherichia coli | ADP + phosphate + arsenite/out | - |
? | |
7.3.2.7 | ATP + H2O + arsenite/in | - |
Escherichia coli JM109 | ADP + phosphate + arsenite/out | - |
? | |
7.3.2.7 | 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 | Escherichia coli | ? | - |
? | |
7.3.2.7 | 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 | Escherichia coli JM109 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
7.3.2.7 | ? | x * 63000, recombinant ArsA, SDS-PAGE | Escherichia coli |
7.3.2.7 | More | ArsA structure analysis and comparison, PDB entry 1F48, overview | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
7.3.2.7 | ArsA ATPase | - |
Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
7.3.2.7 | 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 | Escherichia coli |
7.3.2.7 | 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 | Escherichia coli |
7.3.2.7 | 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 | Escherichia coli |
7.3.2.7 | 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 | Escherichia coli |