(data stored in ACNUC10821 zone)

SWISSPROT: C8U1J3_ECO10

ID   C8U1J3_ECO10            Unreviewed;       516 AA.
AC   C8U1J3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   05-DEC-2018, entry version 44.
DE   SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:BAI29001.1};
GN   Name=cueO {ECO:0000313|EMBL:BAI29001.1};
GN   OrderedLocusNames=ECO103_0123 {ECO:0000313|EMBL:BAI29001.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29001.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29001.1, 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).
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DR   EMBL; AP010958; BAI29001.1; -; Genomic_DNA.
DR   RefSeq; WP_001189608.1; NC_013353.1.
DR   EnsemblBacteria; BAI29001; BAI29001; ECO103_0123.
DR   KEGG; eoh:ECO103_0123; -.
DR   HOGENOM; HOG000096435; -.
DR   KO; K14588; -.
DR   OMA; PHNFHVH; -.
DR   BioCyc; ECOL585395:ECO103_RS00630-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 2.60.40.420; -; 3.
DR   InterPro; IPR001117; Cu-oxidase.
DR   InterPro; IPR011706; Cu-oxidase_2.
DR   InterPro; IPR011707; Cu-oxidase_3.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF00394; Cu-oxidase; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   SUPFAM; SSF49503; SSF49503; 3.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
DR   PRODOM; C8U1J3.
DR   SWISS-2DPAGE; C8U1J3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     28       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        29    516       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002990642.
FT   DOMAIN       55    165       Plastocyanin-like. {ECO:0000259|Pfam:
FT                                PF07732}.
FT   DOMAIN      203    292       Plastocyanin-like. {ECO:0000259|Pfam:
FT                                PF00394}.
FT   DOMAIN      402    516       Plastocyanin-like. {ECO:0000259|Pfam:
FT                                PF07731}.
SQ   SEQUENCE   516 AA;  56654 MW;  353609993A6D173F CRC64;
     MQRRDFLKYS VALGVASALP LWSRAVFAAE RPTLPIPDLL TTDARNRIQL TIGAGQSTFG
     EKTATTWGYN GNLLGPAVKL QRGKAVTVDI YNQLTEETTL HWHGLEVPGE VDGGPQGIIP
     PGGKRSVTLN VDQPAATCWF HPHQHGKTGR QVAMGLAGLV VIEDDEILKL MLPKQWGIDD
     VPVIVQDKKF NADGQIDYQL DVMTAAVGWF GDTLLTNGAI YPQHAAPRGW LRLRLLNGCN
     ARSLNFATSD NRPLYVIASD GGLLPEPVKV SELPVLMGER FEVLVEVNDN KPFDLVTLPV
     SQMGMAIAPF DKPHPVMRIQ PIAISASGAL PDTLSSLPAL PSLEGLTVRK LQLSMDPMLD
     MMGMQMLMEK YGDQAMAGMD HSQMMGHMGH GNMNHMNHGG KFDFHHANKI NGQAFDMNKP
     MFAAAKGQYE RWVISGVGDM MLHPFHIHGT QFRILSENGK PPAAHRAGWK DTVKVEGNVS
     EVLVKFNHNA PKEHAYMAHC HLLEHEDTGM MLGFTV
//

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