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 03-AUG-2022, entry version 118.
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=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., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA 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., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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}.
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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_SDVX01000001.1.
DR AlphaFoldDB; Q8X947; -.
DR SMR; Q8X947; -.
DR STRING; 155864.EDL933_0125; -.
DR EnsemblBacteria; AAG54427; AAG54427; Z0133.
DR EnsemblBacteria; BAB33550; BAB33550; ECs_0127.
DR GeneID; 913706; -.
DR KEGG; ece:Z0133; -.
DR KEGG; ecs:ECs_0127; -.
DR PATRIC; fig|386585.9.peg.225; -.
DR eggNOG; COG2132; Bacteria.
DR HOGENOM; CLU_009100_2_4_6; -.
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_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 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 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..516
FT /note="Multicopper oxidase CueO"
FT /id="PRO_0000002952"
FT DOMAIN 55..165
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 227..292
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 399..516
FT /note="Plastocyanin-like 3"
FT /evidence="ECO:0000255"
FT BINDING 101
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 103
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 141
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 143
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 443
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 446
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 448
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 499
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 500
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 501
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 505
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 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
