(data stored in ACNUC10821 zone)

SWISSPROT: C8U2H0_ECO10

ID   C8U2H0_ECO10            Unreviewed;       834 AA.
AC   C8U2H0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   SubName: Full=Copper transporter CopA {ECO:0000313|EMBL:BAI29328.1};
GN   Name=copA {ECO:0000313|EMBL:BAI29328.1};
GN   OrderedLocusNames=ECO103_0460 {ECO:0000313|EMBL:BAI29328.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29328.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29328.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU362081}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IB subfamily.
CC       {ECO:0000256|RuleBase:RU362081}.
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DR   EMBL; AP010958; BAI29328.1; -; Genomic_DNA.
DR   RefSeq; WP_000083962.1; NC_013353.1.
DR   EnsemblBacteria; BAI29328; BAI29328; ECO103_0460.
DR   KEGG; eoh:ECO103_0460; -.
DR   HOGENOM; HOG000250397; -.
DR   KO; K17686; -.
DR   OMA; NQWSYGH; -.
DR   BioCyc; ECOL585395:ECO103_RS02405-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0030001; P:metal ion transport; IEA:InterPro.
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; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
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; 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; 1.
DR   PROSITE; PS50846; HMA_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; C8U2H0.
DR   SWISS-2DPAGE; C8U2H0.
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Membrane {ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00280,
KW   ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Transmembrane {ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    185    205       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    217    238       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    245    264       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    284    302       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    436    458       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    464    487       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    778    797       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    803    824       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   DOMAIN        4     65       HMA. {ECO:0000259|PROSITE:PS50846}.
FT   DOMAIN      100    163       HMA. {ECO:0000259|PROSITE:PS50846}.
FT   METAL        14     14       {ECO:0000256|PROSITE-ProRule:PRU00280}.
FT   METAL        17     17       {ECO:0000256|PROSITE-ProRule:PRU00280}.
FT   METAL       110    110       {ECO:0000256|PROSITE-ProRule:PRU00280}.
FT   METAL       113    113       {ECO:0000256|PROSITE-ProRule:PRU00280}.
SQ   SEQUENCE   834 AA;  87925 MW;  929F3151482993F8 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 QKGEGESVHA GTVVQDGSVL FRASAVGSHT TLSRIIRMVR
     QAQSSKPEIG QLADKISAVF VPVVVVIALV SAAIWYFFGP APQIVYTLVI ATTVLIIACP
     CALGLATPMS IISGVGRAAE FGVLVRDADA LQRASTLDTV VFDKTGTLTE GKPQVVAVKT
     FADVDEAQAL RLAAALEQGS SHPLARAILD KAGDMQLPQV NGFRTLRGLG VSGEAEGHAL
     LLGNQALLNE QQVGTKAIEA EITAQASQGA 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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