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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=Copper-exporting P-type ATPase A; EC=3.6.3.54; AltName: Full=Cu(+)-exporting ATPase;
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MyHits synonymsCOPA_YERPE , Q8ZCA7 , Q0WCI2 , 8FE8B194BF356A33
match map segment
iprf:HMA_2 iprf:HMA_2 ipat:HMA_1 ipat:HMA_1 iprf:HMA_2 ipfam:HMA ipat:ATPASE_E1_E2 ipfam:HMA ipat:HMA_1 ipfam:HMA  
Legends: 1, ACT_SITE 4-aspartylphosphate intermediate. {ECO:0000305}; 2, Copper. {ECO:0000255|PROSITE- ProRule:PRU00280}; 3, Magnesium. {ECO:0000255|PROSITE- ProRule:PRU00280}; 4, CONFLICT R -> S (in Ref. 2; AAM84670 and 3; AAS61097). {ECO:0000305}; 5, TRANSMEM Helical. {ECO:0000255}; 6, HMA 1. {ECO:0000255|PROSITE- ProRule:PRU00280}; 7, HMA 2. {ECO:0000255|PROSITE- ProRule:PRU00280}; 8, HMA 3. {ECO:0000255|PROSITE- ProRule:PRU00280}; 9, iprf:HMA_2 [T]; 10, ipat:HMA_1 [T]; 11, ipfam:HMA [T]; 12, ipat:ATPASE_E1_E2 [T].
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   10-MAY-2017, entry version 134.
DE   RecName: Full=Copper-exporting P-type ATPase A;
DE            EC=3.6.3.54;
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.,
RA   Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V.,
RA   Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M.,
RA   Simmonds M., Skelton J., 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.,
RA   Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V.,
RA   Straley S.C., McDonough K.A., Nilles M.L., Matson J.S., Blattner F.R.,
RA   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.,
RA   Jin L., Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J.,
RA   Yang H., 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: ATP + H(2)O + Cu(+)(Side 1) = ADP + phosphate
CC       + Cu(+)(Side 2).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) 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_LIXY01000015.1.
DR   RefSeq; YP_002348006.1; NC_003143.1.
DR   ProteinModelPortal; Q8ZCA7; -.
DR   SMR; Q8ZCA7; -.
DR   STRING; 187410.y1093; -.
DR   PRIDE; Q8ZCA7; -.
DR   DNASU; 1146039; -.
DR   EnsemblBacteria; AAM84670; AAM84670; y1093.
DR   EnsemblBacteria; AAS61097; AAS61097; YP_0838.
DR   GeneID; 1175907; -.
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   eggNOG; ENOG4105C59; Bacteria.
DR   eggNOG; COG2217; LUCA.
DR   HOGENOM; HOG000250397; -.
DR   KO; K17686; -.
DR   OMA; FRANAIG; -.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR   CDD; cd00371; HMA; 3.
DR   Gene3D; 1.20.1110.10; -; 1.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 3.
DR   SUPFAM; SSF55008; SSF55008; 3.
DR   SUPFAM; SSF56784; SSF56784; 2.
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; Complete proteome; Copper;
KW   Copper transport; Hydrolase; Ion transport; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    961       Copper-exporting P-type ATPase A.
FT                                /FTId=PRO_0000046325.
FT   TRANSMEM    316    336       Helical. {ECO:0000255}.
FT   TRANSMEM    345    365       Helical. {ECO:0000255}.
FT   TRANSMEM    381    401       Helical. {ECO:0000255}.
FT   TRANSMEM    565    585       Helical. {ECO:0000255}.
FT   TRANSMEM    592    612       Helical. {ECO:0000255}.
FT   TRANSMEM    860    880       Helical. {ECO:0000255}.
FT   TRANSMEM    906    926       Helical. {ECO:0000255}.
FT   TRANSMEM    928    948       Helical. {ECO:0000255}.
FT   DOMAIN        4     65       HMA 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   DOMAIN       70    131       HMA 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   DOMAIN      227    290       HMA 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   ACT_SITE    650    650       4-aspartylphosphate intermediate.
FT                                {ECO:0000305}.
FT   METAL        14     14       Copper. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL        17     17       Copper. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL        80     80       Copper. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL        83     83       Copper. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       237    237       Copper. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       240    240       Copper. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       847    847       Magnesium. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       851    851       Magnesium. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   CONFLICT    376    376       R -> S (in Ref. 2; AAM84670 and 3;
FT                                AAS61097). {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        70    131       iprf:HMA_2 [T]
FT   MYHIT         4     65       iprf:HMA_2 [T]
FT   MYHIT        75    104       ipat:HMA_1 [T]
FT   MYHIT         9     38       ipat:HMA_1 [T]
FT   MYHIT       227    290       iprf:HMA_2 [T]
FT   MYHIT       234    286       ipfam:HMA [T]
FT   MYHIT       650    656       ipat:ATPASE_E1_E2 [T]
FT   MYHIT        74    128       ipfam:HMA [T]
FT   MYHIT       232    261       ipat:HMA_1 [T]
FT   MYHIT         8     62       ipfam:HMA [T]
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
//