(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 115.
DE   RecName: Full=Blue copper oxidase CueO;
DE   AltName: Full=Copper efflux oxidase;
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].
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: Probably involved in periplasmic detoxification of copper by
CC       oxidizing Cu(+) to Cu(2+) and thus preventing its uptake into the
CC       cytoplasm. Possesses phenoloxidase and ferroxidase activities and might
CC       be involved in the production of polyphenolic compounds and the
CC       prevention of oxidative damage in the periplasm (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 4 Cu cations per monomer. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- INDUCTION: By CueR, at increased levels of cytoplasmic cuprous ions.
CC       {ECO:0000305}.
CC   -!- DOMAIN: The methionine-rich domain could provide binding sites for
CC       exogenous copper ions. This methionine-rich region is probably
CC       important for copper tolerance in bacteria.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- DISRUPTION PHENOTYPE: Causes a moderate defect in aerobic growth on
CC       CuSO(4), strongly impairs survival during anaerobic growth on CuSO(4).
CC       {ECO:0000269|PubMed:17768242}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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   SMR; Q8ZRS2; -.
DR   PaxDb; Q8ZRS2; -.
DR   PRIDE; Q8ZRS2; -.
DR   EnsemblBacteria; AAL19132; AAL19132; STM0168.
DR   GeneID; 1251686; -.
DR   KEGG; stm:STM0168; -.
DR   PATRIC; fig|99287.12.peg.178; -.
DR   eggNOG; ENOG4105E3B; Bacteria.
DR   eggNOG; COG2132; LUCA.
DR   HOGENOM; HOG000096435; -.
DR   KO; K14588; -.
DR   OMA; PHNFHVH; -.
DR   PhylomeDB; Q8ZRS2; -.
DR   BioCyc; SENT99287:STM0168-MONOMER; -.
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   Gene3D; 2.60.40.420; -; 3.
DR   InterPro; IPR001117; Cu-oxidase.
DR   InterPro; IPR011706; Cu-oxidase_2.
DR   InterPro; IPR011707; Cu-oxidase_3.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR006311; TAT_signal.
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;
DR   PRODOM; Q8ZRS2.
DR   SWISS-2DPAGE; Q8ZRS2.
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="Blue copper oxidase CueO"
FT                   /id="PRO_0000002954"
FT   DOMAIN          67..163
FT                   /note="Plastocyanin-like 1"
FT   DOMAIN          164..430
FT                   /note="Plastocyanin-like 2"
FT   DOMAIN          431..536
FT                   /note="Plastocyanin-like 3"
FT   COMPBIAS        355..420
FT                   /note="Met-rich"
FT   METAL           101
FT                   /note="Copper 1; type 2"
FT                   /evidence="ECO:0000250"
FT   METAL           103
FT                   /note="Copper 2; type 3"
FT                   /evidence="ECO:0000250"
FT   METAL           141
FT                   /note="Copper 2; type 3"
FT                   /evidence="ECO:0000250"
FT   METAL           143
FT                   /note="Copper 3; type 3"
FT                   /evidence="ECO:0000250"
FT   METAL           463
FT                   /note="Copper 4; type 1"
FT                   /evidence="ECO:0000250"
FT   METAL           466
FT                   /note="Copper 1; type 2"
FT                   /evidence="ECO:0000250"
FT   METAL           468
FT                   /note="Copper 3; type 3"
FT                   /evidence="ECO:0000250"
FT   METAL           519
FT                   /note="Copper 3; type 3"
FT                   /evidence="ECO:0000250"
FT   METAL           520
FT                   /note="Copper 4; type 1"
FT                   /evidence="ECO:0000250"
FT   METAL           521
FT                   /note="Copper 2; type 3"
FT                   /evidence="ECO:0000250"
FT   METAL           525
FT                   /note="Copper 4; type 1"
FT                   /evidence="ECO:0000250"
FT   METAL           530
FT                   /note="Copper 4; type 1"
FT                   /evidence="ECO:0000250"
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
//

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