ID   ARSA2_ECOLX             Reviewed;         583 AA.
AC   P52145;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Arsenical pump-driving ATPase;
DE            EC=7.3.2.7;
DE   AltName: Full=Arsenical resistance ATPase;
DE   AltName: Full=Arsenite-translocating ATPase;
DE   AltName: Full=Arsenite-transporting ATPase;
GN   Name=arsA;
OS   Escherichia coli.
OG   Plasmid IncN R46.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8674982; DOI=10.1111/j.1574-6968.1996.tb08195.x;
RA   Bruhn D.F., Li J., Silver S., Roberto F., Rosen B.P.;
RT   "The arsenical resistance operon of IncN plasmid R46.";
RL   FEMS Microbiol. Lett. 139:149-153(1996).
CC   -!- FUNCTION: Anion-transporting ATPase. Catalyzes the extrusion of the
CC       oxyanions arsenite, antimonite and arsenate. Maintenance of a low
CC       intracellular concentration of oxyanion produces resistance to the
CC       toxic agents.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=arsenite(in) + ATP + H2O = ADP + arsenite(out) + H(+) +
CC         phosphate; Xref=Rhea:RHEA:11348, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29242, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.7;
CC   -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000305}.
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DR   EMBL; U38947; AAB09626.1; -; Genomic_DNA.
DR   AlphaFoldDB; P52145; -.
DR   SMR; P52145; -.
DR   KEGG; ag:AAB09626; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0015446; F:ATPase-coupled arsenite transmembrane transporter activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR025723; Anion-transp_ATPase-like_dom.
DR   InterPro; IPR027541; Ars_ATPase.
DR   InterPro; IPR016300; ATPase_ArsA/GET3.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10803; PTHR10803; 2.
DR   Pfam; PF02374; ArsA_ATPase; 3.
DR   PIRSF; PIRSF001327; Arsenical_pump-driving_ATPase; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR04291; arsen_driv_ArsA; 1.
DR   TIGRFAMs; TIGR00345; GET3_arsA_TRC40; 1.
PE   3: Inferred from homology;
KW   Arsenical resistance; ATP-binding; Nucleotide-binding; Plasmid;
KW   Translocase.
FT   CHAIN           1..583
FT                   /note="Arsenical pump-driving ATPase"
FT                   /id="PRO_0000152252"
FT   BINDING         15..22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         334..341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   583 AA;  63522 MW;  DB0D633DC375C0A2 CRC64;
     MKFLENIPSY LFFTGKGGVG KTSISCATAI RLAELGKRVL LVSTDPASNV GQVFDQTIGN
     TIQPVTAVSG LSALEIDPQD AAQQYRARIV DPIIGLLPDD VVNSISEQLS GACTTEIAAF
     DEFTGLLTDA SLLTRFDHII FDTAPTGHTI RLLQLPGAWS SFIESNPDGA SCLGPMAGLE
     KQREQYAHAV EALSDPERTR LVLVARLQKS TLQEVARTHD ELSAIGLKNQ YLVINGVLPA
     SEEKRDALAA AIWQREQEAL ANLPAGLSDL PTDNLYLQPL NMVGVSALKG LLNEHAEITS
     LPEQSPQNKP ENMSLSVLVD DIARSEHGLI MLMGKGGVGK TTMAAAIAVS LADKGFNVHL
     TTSDPAAHLS TTLNGSLKNL QVSRINPHDE TERYRQHVLE TKGRDLDEAG KRLLEEDLRS
     PCTEEIAVFQ AFSRVIREAG KRFVVMDTAP TGHTLLLLDA TGAYHREIAR KMGDKGHFTT
     PMMQLQDQER TKVLLVTLPE TTPVLEAANL QSDLERAGIH PWGWIINNSL WIAQTQSPLL
     CQRALQERPQ IEVVKNQHAS RIALVPVMAA EPTGIEKLRE LVV