ARSA1_ECOLX
ID ARSA1_ECOLX Reviewed; 583 AA.
AC P08690;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 R773.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3021763; DOI=10.1016/s0021-9258(18)66824-3;
RA Chen C.-M., Misra T.K., Silver S., Rosen B.P.;
RT "Nucleotide sequence of the structural genes for an anion pump. The
RT plasmid-encoded arsenical resistance operon.";
RL J. Biol. Chem. 261:15030-15038(1986).
RN [2]
RP REVIEW.
RX PubMed=1704144; DOI=10.1016/0923-2508(90)90008-e;
RA Rosen B.P.;
RT "The plasmid-encoded arsenical resistance pump: an anion-translocating
RT ATPase.";
RL Res. Microbiol. 141:336-341(1990).
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; J02591; AAA21094.1; -; Genomic_DNA.
DR PIR; A25937; A25937.
DR PDB; 1F48; X-ray; 2.30 A; A=1-583.
DR PDB; 1IHU; X-ray; 2.15 A; A=1-583.
DR PDB; 1II0; X-ray; 2.40 A; A/B=1-583.
DR PDB; 1II9; X-ray; 2.60 A; A/B=1-583.
DR PDBsum; 1F48; -.
DR PDBsum; 1IHU; -.
DR PDBsum; 1II0; -.
DR PDBsum; 1II9; -.
DR AlphaFoldDB; P08690; -.
DR SMR; P08690; -.
DR DIP; DIP-16995N; -.
DR DrugBank; DB02453; Antimonous acid.
DR DrugBank; DB04456; Arsenous acid.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR TCDB; 3.A.4.1.1; the arsenite-antimonite (arsab) efflux family.
DR BioCyc; MetaCyc:MON-21684; -.
DR BRENDA; 7.3.2.7; 2026.
DR EvolutionaryTrace; P08690; -.
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; 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 PANTHER; PTHR10803; PTHR10803; 2.
DR Pfam; PF02374; ArsA_ATPase; 3.
DR PIRSF; PIRSF001327; Arsenical_pump-driving_ATPase; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR04291; arsen_driv_ArsA; 1.
DR TIGRFAMs; TIGR00345; GET3_arsA_TRC40; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arsenical resistance; ATP-binding; Nucleotide-binding;
KW Plasmid; Translocase.
FT CHAIN 1..583
FT /note="Arsenical pump-driving ATPase"
FT /id="PRO_0000152251"
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"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1IHU"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 112..128
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1II0"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1II0"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:1IHU"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 209..225
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 247..261
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 315..323
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 340..353
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 387..403
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 408..417
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 421..432
FT /evidence="ECO:0007829|PDB:1IHU"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 436..440
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 442..447
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 452..460
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 482..486
FT /evidence="ECO:0007829|PDB:1IHU"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 501..516
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 523..530
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 538..555
FT /evidence="ECO:0007829|PDB:1IHU"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:1IHU"
FT STRAND 560..566
FT /evidence="ECO:0007829|PDB:1IHU"
FT HELIX 575..582
FT /evidence="ECO:0007829|PDB:1IHU"
SQ SEQUENCE 583 AA; 63188 MW; 658C5AF65E5E75F5 CRC64;
MQFLQNIPPY LFFTGKGGVG KTSISCATAI RLAEQGKRVL LVSTDPASNV GQVFSQTIGI
TIQAIASVPG LSALEIDPQA AAQQYRARIV DPIKGVLPDD VVSSINEQLS GACTTEIAAF
DEFTGLLTDA SLLTRFDHII FDTAPTGHTI RLLQLPGAWS SFIDSNPEGA SCLGPMAGLE
KQREQYAYAV EALSDPKRTR LVLVARLQKS TLQEVARTHL ELAAIGLKNQ YLVINGVLPK
TEAANDTLAA AIWEREQEAL ANLPADLAGL PTDTLFLQPV NMVGVSALSR LLSTQPVASP
SSDEYLQQRP DIPSLSALVD DIARNEHGLI MLMGKGGVGK TTMAAAIAVR LADMGFDVHL
TTSDPAAHLS MTLNGSLNNL QVSRIDPHEE TERYRQHVLE TKGKELDEAG KRLLEEDLRS
PCTEEIAVFQ AFSRVIREAG KRFVVMDTAP TGHTLLLLDA TGAYHREIAK KMGEKGHFTT
PMMLLQDPER TKVLLVTLPE TTPVLEAANL QADLERAGIH PWGWIINNSL SIADTRSPLL
RMRAQQELPQ IESVKRQHAS RVALVPVLAS EPTGIDKLKQ LAG
