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CUEO_YERPE
ID   CUEO_YERPE              Reviewed;         533 AA.
AC   Q8ZBK0; Q0WBN7;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Multicopper oxidase CueO {ECO:0000250|UniProtKB:P36649};
DE            Short=MCO {ECO:0000250|UniProtKB:P36649};
DE            EC=1.16.3.- {ECO:0000250|UniProtKB:P36649};
DE   AltName: Full=Copper efflux oxidase {ECO:0000250|UniProtKB:P36649};
DE            Short=Cu efflux oxidase {ECO:0000250|UniProtKB:P36649};
DE   AltName: Full=Cuprous oxidase {ECO:0000250|UniProtKB:P36649};
DE   Flags: Precursor;
GN   Name=cueO; OrderedLocusNames=YPO3409, y0777, YP_0276;
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., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   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., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., 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., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   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: Multicopper oxidase involved in copper homeostasis and copper
CC       tolerance under aerobic conditions. Is responsible for the oxidation of
CC       Cu(+) to the less harmful Cu(2+) in the periplasm, thereby preventing
CC       Cu(+) from entering the cytoplasm. {ECO:0000250|UniProtKB:P36649}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Cu(+) + 4 H(+) + O2 = 4 Cu(2+) + 2 H2O;
CC         Xref=Rhea:RHEA:30083, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:29036, ChEBI:CHEBI:49552;
CC         Evidence={ECO:0000250|UniProtKB:P36649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30084;
CC         Evidence={ECO:0000250|UniProtKB:P36649};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P36649};
CC       Note=Binds 4 Cu cations per monomer. {ECO:0000250|UniProtKB:P36649};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P36649}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P36649}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM84364.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAS60552.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL590842; CAL21998.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM84364.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE017042; AAS60552.1; ALT_INIT; Genomic_DNA.
DR   PIR; AC0414; AC0414.
DR   RefSeq; WP_002209340.1; NZ_WUCM01000008.1.
DR   RefSeq; YP_002348301.1; NC_003143.1.
DR   AlphaFoldDB; Q8ZBK0; -.
DR   SMR; Q8ZBK0; -.
DR   IntAct; Q8ZBK0; 2.
DR   STRING; 214092.YPO3409; -.
DR   PaxDb; Q8ZBK0; -.
DR   EnsemblBacteria; AAM84364; AAM84364; y0777.
DR   EnsemblBacteria; AAS60552; AAS60552; YP_0276.
DR   GeneID; 57975300; -.
DR   KEGG; ype:YPO3409; -.
DR   KEGG; ypk:y0777; -.
DR   KEGG; ypm:YP_0276; -.
DR   PATRIC; fig|214092.21.peg.3895; -.
DR   eggNOG; COG2132; Bacteria.
DR   HOGENOM; CLU_009100_2_4_6; -.
DR   OMA; LLPKQWG; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   Gene3D; 2.60.40.420; -; 3.
DR   InterPro; IPR001117; Cu-oxidase.
DR   InterPro; IPR011706; Cu-oxidase_C.
DR   InterPro; IPR045087; Cu-oxidase_fam.
DR   InterPro; IPR011707; Cu-oxidase_N.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   PANTHER; PTHR11709; PTHR11709; 1.
DR   Pfam; PF00394; Cu-oxidase; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   Pfam; PF10518; TAT_signal; 1.
DR   SUPFAM; SSF49503; SSF49503; 3.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Copper; Metal-binding; Oxidoreductase; Periplasm; Reference proteome;
KW   Repeat; Signal.
FT   SIGNAL          1..28
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           29..533
FT                   /note="Multicopper oxidase CueO"
FT                   /id="PRO_0000002955"
FT   DOMAIN          53..166
FT                   /note="Plastocyanin-like 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          221..290
FT                   /note="Plastocyanin-like 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          416..532
FT                   /note="Plastocyanin-like 3"
FT                   /evidence="ECO:0000255"
FT   BINDING         102
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 2 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:P36649"
FT   BINDING         104
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:P36649"
FT   BINDING         142
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:P36649"
FT   BINDING         144
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="3"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:P36649"
FT   BINDING         458
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="4"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:P36649"
FT   BINDING         461
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 2 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:P36649"
FT   BINDING         463
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="3"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:P36649"
FT   BINDING         514
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="3"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:P36649"
FT   BINDING         515
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="4"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:P36649"
FT   BINDING         516
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:P36649"
FT   BINDING         520
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="4"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000250|UniProtKB:P36649"
SQ   SEQUENCE   533 AA;  58328 MW;  ED1570C9E9B1C135 CRC64;
     MHRRDFLKLT AALGAATSLP LWSRAALAAD FSPLPIPPLL QPDANGKINL NIQTGSVVWL
     PSTATQTWGY NGNLLGPAIR LQRGKAVTID ITNALPEATT VHWHGLEIPG EVDGGPQALI
     QPGAKRQVTF AVEQPAATCW FHPHTHSKTG HQVAMGLGGL VLIDDSDSET LPLPKQWGVD
     DIPVILQDKL LDKHGQVDYQ LDVMTAAVGW FGDRMLTNGV PYPQQITPRG WVRLRLLNGC
     NARSLNLALS DGRPMYVIAS DGGLLAEPVV VRELPILMGE RFEVLVDTRD GQSLDLVTLP
     VTQMGMTLAP FDQPLPVLRI QPSLAIGSQV LPESLVVIPE LADVTGVQER WFQLMMDPKL
     DMLGMQALVA RYGMKAMAGM NMNHGDMGAM DHGNRPDMSQ GKMKGMDHGT MNGAPAFNFS
     HANRINGKAF SMTEPAFDAK QGKYEKWTIS GEGDMMLHPF HVHGTQFRIL TENGKPPAEH
     RRGWKDIVRV EGARSEILVR FNYLAPASTP YMAHCHLLEH EDTGMMLGFT VSA
 
 
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