ID   COPA_HELPJ              Reviewed;         745 AA.
AC   Q9ZM69;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Copper-transporting ATPase;
DE            EC=7.2.2.9;
GN   Name=copA; OrderedLocusNames=jhp_0353;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE001439; AAD05935.1; -; Genomic_DNA.
DR   PIR; A71941; A71941.
DR   RefSeq; WP_000664983.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZM69; -.
DR   SMR; Q9ZM69; -.
DR   STRING; 85963.jhp_0353; -.
DR   EnsemblBacteria; AAD05935; AAD05935; jhp_0353.
DR   KEGG; hpj:jhp_0353; -.
DR   PATRIC; fig|85963.30.peg.658; -.
DR   eggNOG; COG2217; Bacteria.
DR   OMA; ITFFGWM; -.
DR   Proteomes; UP000000804; Chromosome.
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   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; 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..745
FT                   /note="Copper-transporting ATPase"
FT                   /id="PRO_0000046174"
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..194
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        216..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        367..379
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        398..685
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        686..705
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        706..716
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        717..735
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        736..745
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..67
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   ACT_SITE        435
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         631
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         635
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
SQ   SEQUENCE   745 AA;  81912 MW;  69E5CD155579C59F CRC64;
     MKESFYIEGM TCTACSSGIE RSLGRKSFVK KIEVSLLNKS ANIEFNENET NLDEIFKLIE
     KLGYSPKKTL AEEKKEFFSP NVKLALAVIF TLFVVYLSMG AMLSPSLLPE SLLTINHHSN
     FLNACLQLIG ALIVMHLGRD FYIQGFKALW HRQPNMSSLI AIGTSAALIS SLWQLYLVYT
     NHYTDQWSYG HYYFESVCVI LMFVMVGKRI ENVSKDKALD AMQALMKNAP KTALKMHNNQ
     QIEVLVDSIV VGDILKVLPG SAIAVDGEII EGEGELDESM LSGEALPVYK KVGDKVFSGT
     LNSNTSFLMK ATQDNKNSTL SQIIEMIHNA QSSKAEISRL ADKVSSVFVP SVIAIAVLAF
     VVWLIIAPKP DFWWNFRTAL EVFVSVLVIS CPCALGLATP MSILVANQKA SSLGLFFKDA
     KSLEKARLVN TIVFDKTGTL TNGKPVVKSI HSNIELLELL SLASSIEKSS EHVIAKGIVE
     YAKERNAPLK DISEVKVKTG FGISAKVDYQ GAKEIIKVGN SEFFNPINTL EIKENGILVF
     VGRAINEKED ELLGAFVLED LPKKGVKEHI AQIKNLGINT FLLSGDNREN VKKCALELGI
     DGYISNAKPQ DKLNKIKELK EKGRIVMMVG DGLNDAPSLA MSDVAVVMAK GSDVSVQAAD
     IVSFNNDIKS VYSAIKLSQA TIKNIKENLF WAFCYNSVFI PLACGVLYKA NIMLSPAIAG
     LAMSLSSVSV VLNSQRLRNF KIKDH