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Database: UniProt
Entry: H0C274_9BURK
LinkDB: H0C274_9BURK
Original site: H0C274_9BURK 
ID   H0C274_9BURK            Unreviewed;       605 AA.
AC   H0C274;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Arsenical pump-driving ATPase {ECO:0000256|PIRNR:PIRNR001327};
DE            EC=7.3.2.7 {ECO:0000256|PIRNR:PIRNR001327};
GN   ORFNames=KYG_18883 {ECO:0000313|EMBL:EHL21277.1};
OS   Acidovorax sp. NO-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL21277.1, ECO:0000313|Proteomes:UP000003485};
RN   [1] {ECO:0000313|EMBL:EHL21277.1, ECO:0000313|Proteomes:UP000003485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NO-1 {ECO:0000313|EMBL:EHL21277.1,
RC   ECO:0000313|Proteomes:UP000003485};
RX   PubMed=22374962; DOI=10.1128/JB.06814-11;
RA   Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT   "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT   Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL   J. Bacteriol. 194:1635-1636(2012).
CC   -!- FUNCTION: Anion-transporting ATPase. {ECO:0000256|PIRNR:PIRNR001327}.
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         Evidence={ECO:0000256|PIRNR:PIRNR001327};
CC   -!- SIMILARITY: Belongs to the arsA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00011040, ECO:0000256|PIRNR:PIRNR001327}.
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DR   EMBL; AGTS01000106; EHL21277.1; -; Genomic_DNA.
DR   RefSeq; WP_008906419.1; NZ_AGTS01000106.1.
DR   AlphaFoldDB; H0C274; -.
DR   STRING; 512030.KYG_18883; -.
DR   PATRIC; fig|512030.4.peg.3732; -.
DR   OrthoDB; 9780677at2; -.
DR   Proteomes; UP000003485; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0015446; F:ATPase-coupled arsenite transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02035; ArsA; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
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   NCBIfam; TIGR04291; arsen_driv_ArsA; 1.
DR   NCBIfam; TIGR00345; GET3_arsA_TRC40; 1.
DR   PANTHER; PTHR10803; ARSENICAL PUMP-DRIVING ATPASE ARSENITE-TRANSLOCATING ATPASE; 1.
DR   PANTHER; PTHR10803:SF3; ATPASE GET3; 1.
DR   Pfam; PF02374; ArsA_ATPase; 2.
DR   PIRSF; PIRSF001327; Arsenical_pump-driving_ATPase; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   Arsenical resistance {ECO:0000256|PIRNR:PIRNR001327};
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001327};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001327};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003485};
KW   Translocase {ECO:0000256|PIRNR:PIRNR001327}.
FT   DOMAIN          17..238
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          338..535
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   605 AA;  63127 MW;  892062B96226BD81 CRC64;
     MTDLHASTVT LGLLARPTRF LFFTGKGGVG KTSLSTAAAI ALADAGRQVL LVSTDAASNL
     DEMLGVPLSN QPVAVPGVPG LHMLNIDPDT AAEAYRQRVL AQLESTATSD ERATVREQLS
     GACTTEIAAF DEFAALLASE GSAIGHVFDH VVFDTAPTGH TLRLLGLPKA WTGFLAGNDR
     GASCLGPHSG LKMQEARFNA ALAALSDPAL TTVVLVTRPD PRPMQEAART ALELRALGLA
     NQRLAINGVF HASRPGQDAV ADAIETLGRQ AMDQMPDALA QLPRDEVPLR AFDTVGLPAL
     RALLAGGAVP LSAPSAVVGA SLQAEPLSSL ADALAAKGHG LIMVMGKGGV GKTTIAAALA
     VGLVQRGHSV HLTTTDPAAH VQSQLDGSLP GLKVGRIDPQ AETQAYIDKI MATRGKALDD
     AGRALLLEDL QSPCTEEVAV FHAFSRVVNE ARSAFVVLDT APTGHSLLLM DATGAYHRQM
     TQQYEGSANS KHIITPLMRL QDADMTHVVI VTLPEVTPVS QAAALQDDLR RAHIEPWAWV
     INKSVAATGT SDPLLQVRLA GEQQQAARIT SGLAQRTYVL PWLVTPPVGV DALGQLAAAP
     VSAAV
//
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