COPA_STAES
ID COPA_STAES Reviewed; 794 AA.
AC Q8CN02;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=SE_2119;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05761.1; -; Genomic_DNA.
DR RefSeq; NP_765674.1; NC_004461.1.
DR RefSeq; WP_001832365.1; NZ_WBME01000013.1.
DR AlphaFoldDB; Q8CN02; -.
DR SMR; Q8CN02; -.
DR STRING; 176280.SE_2119; -.
DR EnsemblBacteria; AAO05761; AAO05761; SE_2119.
DR GeneID; 50017799; -.
DR KEGG; sep:SE_2119; -.
DR PATRIC; fig|176280.10.peg.2070; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_9; -.
DR OMA; ITFFGWM; -.
DR Proteomes; UP000001411; 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; -; 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; 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 PRINTS; PR00120; HATPASE.
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; 1.
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..794
FT /note="Copper-exporting P-type ATPase"
FT /id="PRO_0000350597"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..789
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 4..69
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 71..137
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 494
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 18
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 82
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 85
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 689
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 693
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
SQ SEQUENCE 794 AA; 86101 MW; 83C8B7427C53F567 CRC64;
MANTTLTLDI IGMTCAACSN RIEKKLNRMN HVQAKVNLTT EKATIDYESD DYHLEDFVEQ
IQSLGYDVAV EQVELNINGM TCAACSNRIE KVLNQTQGVQ QATVNLTTEQ ALIKYYPSAT
NTEALIKRIQ NIGYDAETKT SSKAQSNRKK QELKHKRNKL IISAILSLPL LLVMVVHISP
ISIPSILVNP WVQLILSTPV QFIIGWQFYV GAYKNLRNGS ANMDVLVAVG TSAAYFYSIY
EMMMWLTHQT HHPHLYFETS AILITLILLG KYLEARAKSQ TTNALSELLN LQAKEARVIK
ENKEIMLPLD KVKVGDTLLI KPGEKIPVDG KVTKGDTSID ESMLTGESIP VEKSSGDSVI
GSTMNKNGSI MIEATQVGGD TALSHIIKVV EDAQSSKAPI QRLADIISGY FVPIVVSIAV
ITFIIWIIFV HPGQFEPALV SAISVLVIAC PCALGLATPT SIMVGTGRAA ENGILFKGGQ
FVERAHYVDT IVLDKTGTIT NGQPVVTDYV GDNDTLQLLA SAENASEHPL ADAIVTYAKD
KGLNLLDNDT FKSIPGHGIK ATIHQQQILV GNRKLMNDYN ISISNKLNDQ LNHYEHLGQT
AMMIAVDNQI NGIIAVADTV KNDAKQAIKE LRNMNIDVVM LTGDNNRTAQ TIAKQVGIEH
VIAEVLPEEK AHQISLLQDK GKQVAMVGDG INDAPALVKA DIGMAIGTGA EVAIEAADIT
ILGGDLLLVP KAIKASKATI KNIRQNLFWA FGYNVAGIPI AACGLLAPWI AGAAMALSSV
SVVMNALRLK KMKL
