ID   COPA2_HELPX             Reviewed;         741 AA.
AC   Q59467;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Copper-transporting ATPase;
DE            EC=7.2.2.9;
GN   Name=copA;
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A68;
RX   PubMed=9440521; DOI=10.1128/jb.180.2.317-329.1998;
RA   Bayle D., Waengler S., Weitzenegger T., Steinhilber W., Volz J.,
RA   Przybylski M., Schaefer K.P., Sachs G., Melchers K.;
RT   "Properties of the P-type ATPases encoded by the copAP operons of
RT   Helicobacter pylori and Helicobacter felis.";
RL   J. Bacteriol. 180:317-329(1998).
CC   -!- FUNCTION: Probably involved in copper export.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Cu(2+)(in) + H2O = ADP + Cu(2+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:10376, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29036, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.9;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000305}.
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DR   EMBL; U59625; AAB05475.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59467; -.
DR   SMR; Q59467; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043682; F:P-type divalent copper transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0006825; P:copper ion transport; IMP:CACAO.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   Pfam; PF00403; HMA; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF55008; SSF55008; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81660; SSF81660; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Copper; Copper transport; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..741
FT                   /note="Copper-transporting ATPase"
FT                   /id="PRO_0000046172"
FT   TOPO_DOM        1..83
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..124
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..151
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        173..190
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        212..339
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..375
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        394..681
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        682..701
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        702..712
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        713..731
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        732..741
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..67
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   ACT_SITE        431
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         15
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         627
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         631
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
SQ   SEQUENCE   741 AA;  81293 MW;  D1FDEAD11E149DAA CRC64;
     MKESFYIEGM TCTACSSGIE RSLGRKSFVK KIEVSLLNKS ANIEFNENET NLDEIFKLIE
     KLGYSPKKTL AEEKKEFFSP NVKLALAVIF TLFVVYLSMG AMLSPSLLPE SLLTINNHSN
     FLNACLQLIG TLIVMHLGRD FYIQGFKALW HRQPNMSSLI AIGTSAALIS SLWQLYFVYT
     SQWSYGHYYF ESVCVILMFV MVGKRIENVS KDKALDAMQA LMKNAPKTAL KMHNNQQIEV
     LVDSIVVGDI LKVLPGSAIA VDGEIIEGEG ELDESMLSGE ALPVYKKVGD KVFSGTFNSH
     TSFLMKATQD NKNSTLSQIV EMIHNAQSSK AEISRLADKV SSVFVPSVIA IAILAFVVWL
     IIAPKPDFWW NFGIALEVFV SVLVISCPCA LGLATPMSIL VANQKASSLG LFFKDAKSLE
     KARLVNTIVF DKTGTLTNGK PVVKSVHSNI ELLELLSLAG SIEKSSEHVI AKGIVEYAKE
     HNAPLKEMSE VKVKTGFGIS AKTDYQGAKE VIKVGNSEFF NPINALEIQE NGILVFVGRV
     ISEKEDELLG AFVLEDLPKK GVKEHIAQIK KLGINTFLLS GDNRENVKKC ALELGIDGYI
     SNAKPQDKLN KIKELKEKGQ IVMMVGDGLN DAPSLAMSDV AVVMAKGSDV SVQAADIVSF
     NNDIKSVYSA IKLSQATIKN IKENLFWAFC YNSVFIPLAC GVLYKANIML SPAIAGLAMS
     LSSVSVVLNS QRLRNFKIKD H