(data stored in ACNUC7421 zone)

SWISSPROT: CUEO_ECO57

ID   CUEO_ECO57              Reviewed;         516 AA.
AC   Q8X947;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   07-JUN-2017, entry version 103.
DE   RecName: Full=Blue copper oxidase CueO;
DE   AltName: Full=Copper efflux oxidase;
DE   Flags: Precursor;
GN   Name=cueO; OrderedLocusNames=Z0133, ECs0127;
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: Probably involved in periplasmic detoxification of
CC       copper by oxidizing Cu(+) to Cu(2+) and thus preventing its uptake
CC       into the cytoplasm. Possesses phenoloxidase and ferroxidase
CC       activities and might be involved in the production of polyphenolic
CC       compounds and the prevention of oxidative damage in the periplasm
CC       (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 4 Cu cations per monomer. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- INDUCTION: By CueR, at increased levels of cytoplasmic cuprous
CC       ions. {ECO:0000305}.
CC   -!- DOMAIN: The methionine-rich domain could provide binding sites for
CC       exogenous copper ions. This methionine-rich region is probably
CC       important for copper tolerance in bacteria.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000305}.
DR   EMBL; AE005174; AAG54427.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33550.1; -; Genomic_DNA.
DR   PIR; G85495; G85495.
DR   PIR; G90644; G90644.
DR   RefSeq; NP_308154.1; NC_002695.1.
DR   RefSeq; WP_001189614.1; NZ_LPWC02000002.1.
DR   ProteinModelPortal; Q8X947; -.
DR   SMR; Q8X947; -.
DR   STRING; 155864.Z0133; -.
DR   EnsemblBacteria; AAG54427; AAG54427; Z0133.
DR   EnsemblBacteria; BAB33550; BAB33550; BAB33550.
DR   GeneID; 913706; -.
DR   KEGG; ece:Z0133; -.
DR   KEGG; ecs:ECs0127; -.
DR   PATRIC; fig|386585.9.peg.225; -.
DR   eggNOG; ENOG4105E3B; Bacteria.
DR   eggNOG; COG2132; LUCA.
DR   HOGENOM; HOG000096435; -.
DR   KO; K14588; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 4.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8X947.
DR   SWISS-2DPAGE; Q8X947.
KW   Complete proteome; Copper; Metal-binding; Oxidoreductase; Periplasm;
KW   Repeat; Signal.
FT   SIGNAL        1     28       Tat-type signal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00648}.
FT   CHAIN        29    516       Blue copper oxidase CueO.
FT                                /FTId=PRO_0000002952.
FT   DOMAIN       67    163       Plastocyanin-like 1.
FT   DOMAIN      164    410       Plastocyanin-like 2.
FT   DOMAIN      411    516       Plastocyanin-like 3.
FT   COMPBIAS    355    400       Met-rich.
FT   METAL       101    101       Copper 1; type 2. {ECO:0000250}.
FT   METAL       103    103       Copper 2; type 3. {ECO:0000250}.
FT   METAL       141    141       Copper 2; type 3. {ECO:0000250}.
FT   METAL       143    143       Copper 3; type 3. {ECO:0000250}.
FT   METAL       443    443       Copper 4; type 1. {ECO:0000250}.
FT   METAL       446    446       Copper 1; type 2. {ECO:0000250}.
FT   METAL       448    448       Copper 3; type 3. {ECO:0000250}.
FT   METAL       499    499       Copper 3; type 3. {ECO:0000250}.
FT   METAL       500    500       Copper 4; type 1. {ECO:0000250}.
FT   METAL       501    501       Copper 2; type 3. {ECO:0000250}.
FT   METAL       505    505       Copper 4; type 1. {ECO:0000250}.
FT   METAL       510    510       Copper 4; type 1. {ECO:0000250}.
SQ   SEQUENCE   516 AA;  56702 MW;  74D387C799780386 CRC64;
     MQRRDFLKYS VALGVASALP LWSRAVFAAE RPTLPIPDLL TTDARNRIQL TIGAGQSTFG
     EKTATTWGYN GNLLGPAVKL QRGKAVTVDI YNQLTEETTL HWHGLEVPGE VDGGPQGIIP
     PGGKRSVTLN VDQPAATCWF HPHQHGKTGR QVAMGLAGLV VIEDDEILKL MLPKQWGIDD
     VPVIVQDKKF SADGQIDYQL DVMTAAVGWF GDTLLTNGAI YPQHAAPRGW LRLRLLNGCN
     ARSLNFATSD NRPLYVIASD GGLLPEPVKV NELPVLMGER FEVLVEVNDN KPFDLVTLPV
     SQMGMAIAPF DKPHPVMRIQ PIAISASGAL PDTLSSLPAL PSLEGLTVRK LQLSMDPMLD
     MMGMQMLMEK YGDQAMVGMD HSQMMGHMGH GNMNHMNHGG KFDFHHANKI NGQAFDMNKP
     MFAAAKGQYE RWVISGVGDM MLHPFHIHGT QFRILSENGK PPAAHRAGWK DTVKVEGNVS
     EVLVKFNHDA PKERAYMAHC HLLEHEDTGM MLGFTV
//

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