CUEO_SALTI
ID CUEO_SALTI Reviewed; 536 AA.
AC Q8Z9E1;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=STY0190, t0173;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD01326.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO67905.1; -; Genomic_DNA.
DR RefSeq; NP_454781.1; NC_003198.1.
DR RefSeq; WP_000946058.1; NZ_WSUR01000009.1.
DR AlphaFoldDB; Q8Z9E1; -.
DR SMR; Q8Z9E1; -.
DR STRING; 220341.16501454; -.
DR EnsemblBacteria; AAO67905; AAO67905; t0173.
DR KEGG; stt:t0173; -.
DR KEGG; sty:STY0190; -.
DR PATRIC; fig|220341.7.peg.193; -.
DR eggNOG; COG2132; Bacteria.
DR HOGENOM; CLU_009100_2_4_6; -.
DR OMA; LLPKQWG; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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; Repeat; Signal.
FT SIGNAL 1..28
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 29..536
FT /note="Multicopper oxidase CueO"
FT /id="PRO_0000002953"
FT DOMAIN 53..165
FT /note="Plastocyanin-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 229..295
FT /note="Plastocyanin-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 424..536
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 463
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 466
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 468
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 519
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 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"
FT BINDING 521
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 525
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 536 AA; 58624 MW; 2410581D287C3E80 CRC64;
MLRRDFLKYS VALGVASALP LWSRAAFAAE RPALPIPDLL TADASNRMQL IVKAGQSTFA
GKNATTWGYN GNLLGPAVQL HKGKSVTVDI HNQLAEDTTL HWHGLEIPGI VDGGPQGIIP
AGGTRTVTFT PQQRAATCWI HPHKHGKTGR QVAMGLAGLV LIEDDEIRKL RLPKQWGIDD
VPVIIQDKRF SADGQIDYQL DIMTAAVGWF GDTLLTNGAI YPQHSAPKGW LRLRLLNGCN
ARSLNIAASD NRPLYVIASD GGLLAEPVKV TELPLLMGER FEVLVDISDG KAFDLVTLPV
SQMGMAIAPF DKPHPVMRIQ PLRITASGTL PDTLTTMPAL PSLEGLTVRN LKLSMDPRLD
MMGMQMLMKK YGAQAMSGMD HDSMNAHMQG GNMGHGEMDH GNMDHSGMNH GAMGNMNHGG
KFDFHNANFI NGQVFDMNKP MFAAQKGRHE RWVISGVGDM MLHPFHIHGT QFRILSENGK
APAAHRTGWK DTVRVEGGIS EVLVKFDHDA PKEHAYMAHC HLLEHEDTGM MLGFTV
