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 27-MAR-2024, entry version 149.
DE RecName: Full=Multicopper oxidase CueO {ECO:0000250|UniProtKB:P36649};
DE Short=MCO {ECO:0000250|UniProtKB:P36649};
DE EC=1.16.3.4 {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; Pseudomonadota; 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; EC=1.16.3.4;
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; 214092-YPO3409; -.
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; YQLDVMS; -.
DR OrthoDB; 9757546at2; -.
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 CDD; cd04232; CuRO_1_CueO_FtsP; 1.
DR CDD; cd13867; CuRO_2_CueO_FtsP; 1.
DR CDD; cd13890; CuRO_3_CueO_FtsP; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
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; PTHR48267:SF1; BILIRUBIN OXIDASE; 1.
DR PANTHER; PTHR48267; CUPREDOXIN SUPERFAMILY PROTEIN; 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; Cupredoxins; 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
//
