COPA_STAA8
ID COPA_STAA8 Reviewed; 802 AA.
AC Q2FV64;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 121.
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;
DE AltName: Full=Cu(I)-translocating P-type ATPase {ECO:0000303|PubMed:18048940};
GN Name=copA; OrderedLocusNames=SAOUHSC_02873;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION IN COPPER EXPORT, INDUCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS
RP OF CYS-16; CYS-19; CYS-83 AND CYS-86.
RX PubMed=18048940; DOI=10.1099/mic.0.2007/009860-0;
RA Sitthisak S., Knutsson L., Webb J.W., Jayaswal R.K.;
RT "Molecular characterization of the copper transport system in
RT Staphylococcus aureus.";
RL Microbiology 153:4274-4283(2007).
CC -!- FUNCTION: Involved in copper export. Can also probably export ferric
CC and lead ions. {ECO:0000269|PubMed:18048940}.
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 -!- DEVELOPMENTAL STAGE: Highest expression during the exponential growth
CC phase. {ECO:0000269|PubMed:18048940}.
CC -!- INDUCTION: Induced by copper and, to some extent, by ferric and lead
CC ions. {ECO:0000269|PubMed:18048940}.
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; CP000253; ABD31871.1; -; Genomic_DNA.
DR RefSeq; WP_000024127.1; NZ_LS483365.1.
DR RefSeq; YP_501328.1; NC_007795.1.
DR AlphaFoldDB; Q2FV64; -.
DR SMR; Q2FV64; -.
DR STRING; 1280.SAXN108_2808; -.
DR EnsemblBacteria; ABD31871; ABD31871; SAOUHSC_02873.
DR GeneID; 3921544; -.
DR KEGG; sao:SAOUHSC_02873; -.
DR PATRIC; fig|93061.5.peg.2597; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_9; -.
DR OMA; ITFFGWM; -.
DR PRO; PR:Q2FV64; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Copper; Copper transport; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..802
FT /note="Copper-exporting P-type ATPase"
FT /id="PRO_0000350593"
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"
FT MUTAGEN 16
FT /note="C->A: Abolishes copper binding; when associated with
FT A-19; A-83 and A-86."
FT /evidence="ECO:0000269|PubMed:18048940"
FT MUTAGEN 19
FT /note="C->A: Abolishes copper binding; when associated with
FT A-16; A-83 and A-86."
FT /evidence="ECO:0000269|PubMed:18048940"
FT MUTAGEN 83
FT /note="C->A: Abolishes copper binding; when associated with
FT A-16; A-19 and A-86."
FT /evidence="ECO:0000269|PubMed:18048940"
FT MUTAGEN 86
FT /note="C->A: Abolishes copper binding; when associated with
FT A-16; A-19 and A-83."
FT /evidence="ECO:0000269|PubMed:18048940"
SQ SEQUENCE 802 AA; 86744 MW; 23B26C2ED46A9E69 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
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 TNGRPVVTDY HGDNQTLQLL ATAEKDSEHP LAEAIVNYAK
EKQLILTETT 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
