ID   COPA_STAAR              Reviewed;         802 AA.
AC   Q6GDP1;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Copper-exporting P-type ATPase;
DE            EC=7.2.2.8;
DE   AltName: Full=Copper-exporting P-type ATPase A;
DE   AltName: Full=Cu(+)-exporting ATPase;
GN   Name=copA; OrderedLocusNames=SAR2637;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Involved in copper export. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC         ChEBI:CHEBI:456216; EC=7.2.2.8;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
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; BX571856; CAG41616.1; -; Genomic_DNA.
DR   RefSeq; WP_000024146.1; NC_002952.2.
DR   AlphaFoldDB; Q6GDP1; -.
DR   SMR; Q6GDP1; -.
DR   KEGG; sar:SAR2637; -.
DR   HOGENOM; CLU_001771_0_3_9; -.
DR   OMA; ITFFGWM; -.
DR   OrthoDB; 237367at2; -.
DR   Proteomes; UP000000596; 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:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR   CDD; cd00371; HMA; 2.
DR   Gene3D; 3.40.1110.10; -; 2.
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; IPR006122; HMA_Cu_ion-bd.
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; 2.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF55008; SSF55008; 2.
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   TIGRFAMs; TIGR00003; TIGR00003; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 2.
DR   PROSITE; PS50846; HMA_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Copper; Copper transport; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Repeat; Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..802
FT                   /note="Copper-exporting P-type ATPase"
FT                   /id="PRO_0000350587"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        748..767
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        771..790
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          5..70
FT                   /note="HMA 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   DOMAIN          72..138
FT                   /note="HMA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   ACT_SITE        495
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         19
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         83
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         86
FT                   /ligand="Cu(+)"
FT                   /ligand_id="ChEBI:CHEBI:49552"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         690
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         694
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
SQ   SEQUENCE   802 AA;  86766 MW;  B4DCBE917908932D CRC64;
     MANTKKTTLD ITGMTCAACS NRIEKKLNKL DDVNAQVNLT TEKATVEYNP DRHDVQEFIN
     TIQHLGYGVA VETVELDITG MTCAACSSRI EKVLNKMDGV QNATVNLTTE QAKVDYYPEE
     TDADKLVTRI QKLGYDASIK DNNRDQTSRK AEALQHKLIK LIISAVLSLP LLMLMFVHLF
     NMHIPALFTN PWFQFILATP VQFIIGWQFY VGAYKNLRNG GANMDVLVAV GTSAAYFYSI
     YEMVRWLNGS TTQPHLYFET SAVLITLILF GKYLEARAKS QTTNALGELL SLQAKEARIL
     KDGNEVMIPL NEVHVGDTLI VKPGEKIPVD GKIIKGMTAI DESMLTGESI PVEKNVDDTV
     IGSTMNKNGT ITMTATKVGG DTALANIIKV VEEAQSSKAP IQRLADIISG YFVPIVVGIA
     LLTFIVWITL VTPGTFEPAL VASISVLVIA CPCALGLATP TSIMVGTGRA AENGILFKGG
     EFVERTHQID TIVLDKTGTI TNGCPVVTDY HGDDQTLQLL ATAEKDSEHP LAEAIVNYAK
     EKQLTLTETT TFKAVPGHGI EATIDHHHIL VGNRKLMADN DISLPKHISD DLTHYERDGK
     TAMLIAVNYS LTGIIAVADT VKDHAKDAIK QLHDMGIEVA MLTGDNKNTA QAIAKQVGID
     TVIADILPEE KAAQITKLQQ QGKKVAMVGD GVNDAPALVK ADIGIAIGTG TEVAIEAADI
     TILGGDLMLI PKAIYASKAT IRNIRQNLFW AFGYNIAGIP IAALGLLAPW VAGAAMALSS
     VSVVTNALRL KKMRLEPRRK DA