COPA_YERPE
ID COPA_YERPE Reviewed; 961 AA.
AC Q8ZCA7; Q0WCI2;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 161.
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=YPO3086, y1093, YP_0838;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(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:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; AL590842; CAL21688.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84670.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS61097.1; -; Genomic_DNA.
DR PIR; AE0375; AE0375.
DR RefSeq; WP_002208579.1; NZ_UHIZ01000001.1.
DR RefSeq; YP_002348006.1; NC_003143.1.
DR AlphaFoldDB; Q8ZCA7; -.
DR SMR; Q8ZCA7; -.
DR STRING; 214092.YPO3086; -.
DR PaxDb; Q8ZCA7; -.
DR DNASU; 1146039; -.
DR EnsemblBacteria; AAM84670; AAM84670; y1093.
DR EnsemblBacteria; AAS61097; AAS61097; YP_0838.
DR GeneID; 57975618; -.
DR KEGG; ype:YPO3086; -.
DR KEGG; ypk:y1093; -.
DR KEGG; ypl:CH46_2014; -.
DR KEGG; ypm:YP_0838; -.
DR KEGG; ypv:BZ15_442; -.
DR KEGG; ypw:CH59_2980; -.
DR PATRIC; fig|214092.21.peg.3541; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_5_0_6; -.
DR OMA; ITFFGWM; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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; 3.
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; 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; 3.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 3.
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 PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 3.
DR PROSITE; PS50846; HMA_2; 3.
PE 3: Inferred from homology;
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..961
FT /note="Copper-exporting P-type ATPase"
FT /id="PRO_0000046325"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 860..880
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 906..926
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 928..948
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 3..64
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 69..130
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 226..289
FT /note="HMA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT REGION 131..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 650
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305"
FT BINDING 14
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 17
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 80
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
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 237
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 240
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 847
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 851
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT CONFLICT 376
FT /note="R -> S (in Ref. 2; AAM84670 and 3; AAS61097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 961 AA; 101409 MW; 8FE8B194BF356A33 CRC64;
MLQTTLLALQ GLSCMNCAQR VKAALESRED VHHAEVNVHY AKVTGEADTH ALIETIKQTG
YQATEAQTPD VELHLSGLSC GHCTETVRKA LEAVSGVISA DVTLESANVY GKADIQTLIA
AVEQAGYHAT QQGIDSPKTE PLTHSAQSQP ESLAAAPNTV PATNVALATS TVSDTNTVLP
TNTALPTNTT STTSTADTAS ATSTAPVINP LPVTESVAQP AASEGESVQL LLTGMSCASC
VSKVQNALQR VDGVQVARVN LAERSALVTG TQNNEALIAA VKNAGYGAEI IEDEGERRER
QQQMSQASMK RFQWQAALGL LLGIPLMAWG LFGGSMTLTP ETQTPWLIIG IITLLVMIFA
GGHFYRNAWV SLKNGRATMD TLVALGTGAA WIYSITVNIW PDVFPMEARH LYYEASAMII
GLINLGHAME QRARQRSSNA LERLLDLAPP TAKLVTDDGE KVIPLADVQL GMILRLTTGD
RVPVDGEIVQ GEVWMDEAML TGEPIPQQKS VGDIVHAGTQ VQDGTVQFRA SAIGSQTTLA
RIIKLVRQAQ SSKPEIGKLA DRISAVFVPT VVVIAIVAGL IWYFFGPQPQ LVYTLVVATT
VLIIACPCAL GLATPMSIIS GVGRAAEFGV LVRDADALQQ ASNLDTLVFD KTGTLTEGHP
QVVAIHTFNG VSEQQALGWA AALETGSNHP LARAILQRAE GLTLATASQF RTLRGLGVSG
EVDGIPLLLG NNRLLEEQQI DTRELQSLIQ QQAESGATPV ILTANGKPAA LLSIRDPLRE
DSIGALQRLH QLGYSLVMLT GDNPITANAI AKEAGIDRVI AGVLPDGKAD AIKQLQAAGH
KVAMIGDGIN DAPALAQADV GIAMGGGSDI AIETAAITLM RHSLYGVVDA VELSKATLRN
MKQNLLGAFF YNALGIPIAA GILYPFTGTL LSPVVAGAAM ALSSITVVSN ANRLLRFKPK
Q
