(data stored in ACNUC7421 zone)

SWISSPROT: COPA_ECO57

ID   COPA_ECO57              Reviewed;         834 AA.
AC   Q8XD24;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   05-JUL-2017, entry version 123.
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=Z0604, ECs0537;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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}.
DR   EMBL; AE005174; AAG54833.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33960.1; -; Genomic_DNA.
DR   PIR; A90696; A90696.
DR   PIR; E85546; E85546.
DR   RefSeq; NP_308564.1; NC_002695.1.
DR   RefSeq; WP_000083954.1; NZ_MWVM01000009.1.
DR   ProteinModelPortal; Q8XD24; -.
DR   SMR; Q8XD24; -.
DR   STRING; 155864.Z0604; -.
DR   EnsemblBacteria; AAG54833; AAG54833; Z0604.
DR   EnsemblBacteria; BAB33960; BAB33960; BAB33960.
DR   GeneID; 914641; -.
DR   KEGG; ece:Z0604; -.
DR   KEGG; ecs:ECs0537; -.
DR   PATRIC; fig|386585.9.peg.644; -.
DR   eggNOG; ENOG4105C59; Bacteria.
DR   eggNOG; COG2217; LUCA.
DR   HOGENOM; HOG000250397; -.
DR   KO; K17686; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; 2.
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; PF00403; HMA; 2.
DR   PRINTS; PR00120; HATPASE.
DR   SUPFAM; SSF55008; SSF55008; 2.
DR   SUPFAM; SSF56784; SSF56784; 2.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81665; SSF81665; 3.
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; 1.
DR   PROSITE; PS50846; HMA_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; Q8XD24.
DR   SWISS-2DPAGE; Q8XD24.
KW   ATP-binding; Cell membrane; Complete proteome; Copper;
KW   Copper transport; Hydrolase; Ion transport; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    834       Copper-exporting P-type ATPase A.
FT                                /FTId=PRO_0000046321.
FT   TRANSMEM    187    207       Helical. {ECO:0000255}.
FT   TRANSMEM    218    238       Helical. {ECO:0000255}.
FT   TRANSMEM    254    274       Helical. {ECO:0000255}.
FT   TRANSMEM    284    304       Helical. {ECO:0000255}.
FT   TRANSMEM    438    458       Helical. {ECO:0000255}.
FT   TRANSMEM    464    484       Helical. {ECO:0000255}.
FT   TRANSMEM    779    799       Helical. {ECO:0000255}.
FT   TRANSMEM    801    821       Helical. {ECO:0000255}.
FT   DOMAIN        4     65       HMA 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   DOMAIN      100    163       HMA 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   ACT_SITE    523    523       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       110    110       Copper. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       113    113       Copper. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       720    720       Magnesium. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
FT   METAL       724    724       Magnesium. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00280}.
SQ   SEQUENCE   834 AA;  88005 MW;  B4789F2CCF12E9FB CRC64;
     MSQTIDLTLD GLSCGHCVKR VKESLEQRPD VEQADVSITE AHVTGTASAE QLIETIKQAG
     YDASVSHPKA KPLAESSIPS EALTAVSEAL PAATADDDDS QQLLLSGMSC ASCVTRVQNA
     LQSVPGVTQA RVNLAERTAL VMGSASPQDL VQAVEKAGYG AEAIEDDAKR RERQQETAVA
     TMKRFRWQAI VALAVGIPVM VWGMIGDNMM VTADNRSLWL VIGLITLAVM VFAGGHFYRS
     AWKSLLNGAA TMDTLVALGT GVAWLYSMSV NLWPQWFPME ARHLYYEASA MIIGLINLGH
     MLEARARQRS SKALEKLLDL TPPTARLVTD EGEKSVPLAE VQPGMLLRLT TGDRVPVDGE
     ITQGEAWLDE AMLTGEPIPQ QKGEGDSVHA GTVVQDGSVL FRASAVGSHT TLSRIIRMVR
     QAQSSKPEIG QLADKISAVF VPVVVVIALV SAAIWYFFGP APQIVYTLVI ATTVLIIACP
     CALGLATPMS IISGVGRAAE FGVLVRDADA LQRASTLDTV VFDKTGTLTE GKPQVVAVKT
     FADFDEAQAL RLAAALEQGS SHPLARAILD KASDMQLPQV NGFRTLRGLG VSGEAEGHAL
     LLGNQALLND QQVDTKAIEA DISAQASQGA TPVLLAVDGK AVALLAVRDP LRSDSVAALQ
     RLHKAGYRLV MLTGDNPTTA NAIAKEAGID EVIAGVLPDG KAEAIKRLQS EGRQVAMVGD
     GINDAPALAQ ADVGIAMGGG SDVAIETAAI TLMRHSLMGV ADALAISRAT LRNMKQNLLG
     AFIYNSIGIP VAAGILWPFT GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE
//

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