CUEO_SALTY
ID CUEO_SALTY Reviewed; 536 AA.
AC Q8ZRS2; Q938E6;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
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; Synonyms=cuiD {ECO:0000303|PubMed:12442888};
GN OrderedLocusNames=STM0168;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12442888;
RA Lim S.Y., Joe M.H., Song S.S., Lee M.H., Foster J.W., Park Y.K., Choi S.Y.,
RA Lee I.S.;
RT "CuiD is a crucial gene for survival at high copper environment in
RT Salmonella enterica serovar Typhimurium.";
RL Mol. Cells 14:177-184(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION IN COPPER TOLERANCE, REGULATION BY CUER, INDUCTION BY COPPER, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=17768242; DOI=10.1099/mic.0.2007/006536-0;
RA Espariz M., Checa S.K., Perez Audero M.E., Pontel L.B., Soncini F.C.;
RT "Dissecting the Salmonella response to copper.";
RL Microbiology 153:2989-2997(2007).
CC -!- FUNCTION: Multicopper oxidase involved in copper homeostasis and copper
CC tolerance under both aerobic and anaerobic conditions (PubMed:12442888,
CC PubMed:17768242). Is responsible for the oxidation of Cu(+) to the less
CC harmful Cu(2+) in the periplasm, thereby preventing Cu(+) from entering
CC the cytoplasm (By similarity). {ECO:0000250|UniProtKB:P36649,
CC ECO:0000269|PubMed:12442888, ECO:0000269|PubMed:17768242}.
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 -!- INDUCTION: By CueR, at increased levels of cytoplasmic cuprous ions.
CC {ECO:0000269|PubMed:17768242}.
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 -!- DISRUPTION PHENOTYPE: Mutant is very sensitive to copper after copper
CC shock (PubMed:12442888). Causes a moderate defect in aerobic growth on
CC CuSO(4), strongly impairs survival during anaerobic growth on CuSO(4)
CC (PubMed:17768242). {ECO:0000269|PubMed:12442888,
CC ECO:0000269|PubMed:17768242}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; AY053392; AAL15149.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19132.1; -; Genomic_DNA.
DR RefSeq; NP_459173.1; NC_003197.2.
DR RefSeq; WP_000946047.1; NC_003197.2.
DR AlphaFoldDB; Q8ZRS2; -.
DR SMR; Q8ZRS2; -.
DR STRING; 99287.STM0168; -.
DR PaxDb; Q8ZRS2; -.
DR EnsemblBacteria; AAL19132; AAL19132; STM0168.
DR GeneID; 1251686; -.
DR KEGG; stm:STM0168; -.
DR PATRIC; fig|99287.12.peg.178; -.
DR HOGENOM; CLU_009100_2_4_6; -.
DR OMA; LLPKQWG; -.
DR PhylomeDB; Q8ZRS2; -.
DR BioCyc; SENT99287:STM0168-MON; -.
DR SABIO-RK; Q8ZRS2; -.
DR Proteomes; UP000001014; 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 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 1: Evidence at protein level;
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..536
FT /note="Multicopper oxidase CueO"
FT /id="PRO_0000002954"
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"
FT CONFLICT 322..323
FT /note="LR -> AA (in Ref. 1; AAL15149)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="L -> F (in Ref. 1; AAL15149)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 536 AA; 58625 MW; E4C04555AF6F21DF CRC64;
MLRRDFLKYS VALGVASALP LWSRAAFAAE RPALPIPDLL TADASNRMQL IVKAGQSTFA
GKNATTWGYN GNLLGPAVQL HKGKSVTVDI HNQLAEDTTL HWHGLEIPGI VDGGPQGIIP
AGGTRTVTFT PEQRAATCWI 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
