ARSA_ACIMA
ID ARSA_ACIMA Reviewed; 583 AA.
AC O50593;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Acidiphilium multivorum (strain DSM 11245 / JCM 8867 / NBRC 100883 / AIU
OS 301).
OG Plasmid pKW301.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=926570;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 11245 / JCM 8867 / NBRC 100883 / AIU 301;
RX PubMed=9464374; DOI=10.1128/aem.64.2.411-418.1998;
RA Suzuki K., Wakao N., Kimura T., Sakka K., Ohmiya K.;
RT "Expression and regulation of the arsenic resistance operon of Acidiphilium
RT multivorum AIU 301 plasmid pKW301 in Escherichia coli.";
RL Appl. Environ. Microbiol. 64:411-418(1998).
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; AB004659; BAA24822.1; -; Genomic_DNA.
DR AlphaFoldDB; O50593; -.
DR SMR; O50593; -.
DR PRIDE; O50593; -.
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_0000152250"
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; 63196 MW; 306D82745B2F690A CRC64;
MKLLQNIPPY LFFTGKGGVG KTSISCATAI HLAEQGKRVL LVSTDPASNV GQVFDLAIGN
TIRPVTAVPG LSALEIDPQE AARQYRARIV DPIKGLLPDD VVNSISEQLS GACTTEIAAF
DEFTGLLTDA SLLTRFDHII FDTAPTGHTI RLLQLPGAWS SFIESNPDGA SCLGPMAGLE
KQREQYAHAV EALSDPERTR LVLVARLQNS TLQEVARTHE ELAEIGLKNQ YLVINGVLPE
AEAEHDALAA AIWQREQEAL ANLPAGLSEL PTDTLLLQPV NMVGVSALKG LLATRSEALP
LPVTNILYTP ENLSLSGLVD DIARSEHGLI MLMGKGGVGK TTMAAAIAVR LADMGFDVHL
TTSDPAAHLS TTLNGSLKNL QVSRINPHDE TERYRQHVLE TKGRDLDEAG KRLLEEDLRS
PCTEEIAVFQ AFSRVIREAG KRFVVMDTAP TGHTLLLLDA TGAYHREIAK KMGSKGHFTT
PMMQLQDPDR TKVLLVTLPE TTPVLEAANL QADLERAGIH PWGWIINNSL SIADTRSPLL
CQRAQQELPQ IEAVKNQHAD RIALVPVLAS EPAGIEKLRE LMS
