ID   COPA_STAA2              Reviewed;         802 AA.
AC   A6U4T8;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=SaurJH1_2633;
OS   Staphylococcus aureus (strain JH1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=359787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JH1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Tomasz A., Richardson P.;
RT   "Complete sequence of chromosome of Staphylococcus aureus subsp. aureus
RT   JH1.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000736; ABR53456.1; -; Genomic_DNA.
DR   RefSeq; WP_000024139.1; NC_009632.1.
DR   AlphaFoldDB; A6U4T8; -.
DR   SMR; A6U4T8; -.
DR   KEGG; sah:SaurJH1_2633; -.
DR   HOGENOM; CLU_001771_0_3_9; -.
DR   OMA; ITFFGWM; -.
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_0000350585"
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;  86773 MW;  2BCC0B7D7E173DDC CRC64;
     MANTKKTTLD ITGMTCAACS NRIEKKLNKL DDVNAQVNLT TEKATVEYNP DQHDVQEFIN
     TIQHLGYGVT VETVELDITG MTCAACSSRI EKVLNKMNGV QNATVNLTTE QAKVDYYPEE
     TDADKLVTRI QKLGYDASIK DNNKDQTSRK AEALQHKLIK LIISAVLSLP LLMLMFVHLF
     NMHIPALFTN PWFQFILATP VQFIIGWQFY VGAYKNLRNG GANMDVLVAV GTSAAYFYSI
     YEMVRWLNGS TTQPHLYFET SAVLLTLILF GKYLEARAKS QTTNALGELL SLQAKEARIL
     KDGNEVMIPL NEVHVGDTLI VKPGEKIPVD GKIIKGMTAI DESMLTGESI PVEKNVDDTV
     IGSTMNKNGT ITMTATKVGG DTALANIIKV VEEAQSSKAP IQRLADIISG YFVPIVVGIA
     LLIFIVWITL VTPGTFEPAL VASISVLVIA CPCALGLATP TSIMVGTGRA AENGILFKGG
     EFVERTHQID TIVLDKTGTI TNGRPVVTDY HGDNQTLQLL ATAEKDSEHP LAEAIVNYAK
     EKQLTLTETT TFKAVPGHGI EATIDHHHIL VGNRKLMADN DISLPKHISD DLTHYERDGK
     TAMLIAVNYS LTGIIAVADT VKDHAKDAIK QLHDMGIEVA MLTGDNKNTA QAIAKQVGID
     TVIADILPEE KAAQIAKLQQ QGKKVAMVGD GVNDAPALVK ADIGIAIGTG TEVAIEAADI
     TILGGDLMLI PKAIYASKAT IRNIRQNLFW AFGYNIAGIP IAALGLLAPW VAGAAMALSS
     VSVVTNALRL KKMRLEPRRK DA