COPA_STAAB
ID COPA_STAAB Reviewed; 802 AA.
AC Q2YWA3;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=SAB2431;
OS Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=273036;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bovine RF122 / ET3-1;
RX PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT "Molecular correlates of host specialization in Staphylococcus aureus.";
RL PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI82119.1; -; Genomic_DNA.
DR RefSeq; WP_000024121.1; NC_007622.1.
DR AlphaFoldDB; Q2YWA3; -.
DR SMR; Q2YWA3; -.
DR KEGG; sab:SAB2431; -.
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_0000350583"
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; 86716 MW; 3950492E6BC73E6E CRC64;
MANTKKTTLD ITGMTCAACS NRIEKKLNKL DDVNAQVNLT TEKATVEYNP DQHDVQEFIN
TIQHLGYGVA VETVELDITG MTCAACSSRI EKVLNKMDGV QNATVNLTTE QAKVDYYPEE
TDADKLVTRI QKLGYDASIK DNNKDQTSRK AEALQHKLIK LIISAVLSLP LLMLMFVHLF
NMHIPALFTN PWFQFILATP VQFIIGWQFY VGAYKNLRNG GANMDVLVAV GTSAAYFYSI
YEMIRWLNGS TTQPHLYFET SAVLITLILF GKYLEARAKS QTTNALGELL SLQAKEARIL
KDGNELMIPL NEVHVGDTLI VKPGEKIPVD GKIIKGMTAI DESMLTGESI PVEKNVDDTV
IGSTMNKNGT ITMTATKVGG DTALANIIKV VEEAQSSKAP IQRLADIISG YFVPIVVGIA
LLTFIVWITL VTPGTFEPAL VASISVLVIA CPCALGLATP TSIMVGTGRA AENGILFKGG
EFVERTHQID TIVLDKTGTI TNGRPVVTDY HGDDQTLQLL ATAEKDSEHP LAEAIVNYAK
EKQLTLTETT TFKAVPGHGI EATIDHHHIL VGNRKLMADN DISLPKHISD DLTHYERDGK
TAMLIAVNYS LTGIIAVADT LKNHAKDAIK QLHDMGIEVA MLTGDNKNTA QAIAKQVGID
TVIADILPEE KAAQIAKLQQ QGKKVAMVGD GVNDAPALVK ADIGIAIGTG TEVAIEAAGI
TILGGDLMLI PKAIYASKAT IRNIRQNLFW AFGYNIAGIP IAALGLLAPW VAGAAMALSS
VSVVTNALRL KKMRLEPRRK DA
