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Blue copper oxidase CueO (Copper efflux oxidase)

 CUEO_ECOLI              Reviewed;         516 AA.
P36649; P75655; Q8KMZ0;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
25-OCT-2017, entry version 154.
RecName: Full=Blue copper oxidase CueO;
AltName: Full=Copper efflux oxidase;
Flags: Precursor;
Name=cueO; Synonyms=yacK; OrderedLocusNames=b0123, JW0119;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8202364; DOI=10.1093/nar/22.9.1637;
Fujita N., Mori H., Yura T., Ishihama A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
2.4-4.1 min (110,917-193,643 bp) region.";
Nucleic Acids Res. 22:1637-1639(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
PROTEIN SEQUENCE OF 29-40.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[5]
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=B / BL21;
PubMed=10493123;
DOI=10.1002/(SICI)1522-2683(19990801)20:11<2181::AID-ELPS2181>3.0.CO;2-Q;
Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
"Enrichment of low abundance proteins of Escherichia coli by
hydroxyapatite chromatography.";
Electrophoresis 20:2181-2195(1999).
[6]
POSSIBLE FUNCTION IN COPPER HOMEOSTASIS.
PubMed=11222619; DOI=10.1128/JB.183.6.2145-2147.2001;
Grass G., Rensing C.;
"Genes involved in copper homeostasis in Escherichia coli.";
J. Bacteriol. 183:2145-2147(2001).
[7]
POSSIBLE FUNCTION IN COPPER HOMEOSTASIS.
STRAIN=K12;
PubMed=11399769; DOI=10.1074/jbc.M104122200;
Outten F.W., Huffman D.L., Hale J.A., O'Halloran T.V.;
"The independent cue and cus systems confer copper tolerance during
aerobic and anaerobic growth in Escherichia coli.";
J. Biol. Chem. 276:30670-30677(2001).
[8]
CHARACTERIZATION.
STRAIN=K12 / DH5-alpha;
PubMed=10915804; DOI=10.1074/jbc.M006508200;
Outten F.W., Outten C.E., Hale J.A., O'Halloran T.V.;
"Transcriptional activation of an Escherichia coli copper efflux
regulon by the chromosomal merR homologue, cueR.";
J. Biol. Chem. 275:31024-31029(2000).
[9]
CHARACTERIZATION.
STRAIN=K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
PubMed=11466290; DOI=10.1128/JB.183.16.4866-4875.2001;
Kim C., Lorenz W.W., Hoopes J.T., Dean J.F.D.;
"Oxidation of phenolate siderophores by the multicopper oxidase
encoded by the Escherichia coli yacK gene.";
J. Bacteriol. 183:4866-4875(2001).
[10]
CHARACTERIZATION, AND MUTAGENESIS OF 500-CYS-HIS-501.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=11527384; DOI=10.1006/bbrc.2001.5474;
Grass G., Rensing C.;
"CueO is a multi-copper oxidase that confers copper tolerance in
Escherichia coli.";
Biochem. Biophys. Res. Commun. 286:902-908(2001).
[11]
EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
PubMed=17218314; DOI=10.1074/jbc.M610507200;
Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P.,
Ribnicky B., Palmer T., Georgiou G.;
"Export pathway selectivity of Escherichia coli twin arginine
translocation signal peptides.";
J. Biol. Chem. 282:8309-8316(2007).
[12]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=11867755; DOI=10.1073/pnas.052710499;
Roberts S.A., Weichsel A., Grass G., Thakali K., Hazzard J.T.,
Tollin G., Rensing C., Montfort W.R.;
"Crystal structure and electron transfer kinetics of CueO, a
multicopper oxidase required for copper homeostasis in Escherichia
coli.";
Proc. Natl. Acad. Sci. U.S.A. 99:2766-2771(2002).
-!- FUNCTION: Probably involved in periplasmic detoxification of
copper by oxidizing Cu(+) to Cu(2+) and thus preventing its uptake
into the cytoplasm. Possesses phenoloxidase and ferroxidase
activities and might be involved in the production of polyphenolic
compounds and the prevention of oxidative damage in the periplasm.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Note=Binds 4 Cu cations per monomer.;
-!- SUBUNIT: Monomer. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Periplasm. Note=It is exported via the Tat
pathway.
-!- INDUCTION: By CueR, at increased levels of cytoplasmic cuprous
ions.
-!- DOMAIN: The methionine-rich domain could provide binding sites for
exogenous copper ions. This methionine-rich region is probably
important for copper tolerance in bacteria.
-!- PTM: Exported by the Tat system. The position of the signal
peptide cleavage has been experimentally proven. Can also be
exported by the Sec system.
-!- MISCELLANEOUS: This protein is sensitive to oxygen deprivation. It
probably plays a significant role in copper efflux under aerobic
conditions.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U00096; AAC73234.1; -; Genomic_DNA.
EMBL; AP009048; BAB96698.2; -; Genomic_DNA.
PIR; C64735; C64735.
RefSeq; NP_414665.1; NC_000913.3.
RefSeq; WP_001189647.1; NZ_LN832404.1.
PDB; 1KV7; X-ray; 1.40 A; A=29-516.
PDB; 1N68; X-ray; 1.70 A; A=29-516.
PDB; 1PF3; X-ray; 1.50 A; A=29-516.
PDB; 2FQD; X-ray; 2.40 A; A=29-516.
PDB; 2FQE; X-ray; 1.92 A; A=29-516.
PDB; 2FQF; X-ray; 2.00 A; A=29-516.
PDB; 2FQG; X-ray; 2.30 A; A=29-516.
PDB; 2YXV; X-ray; 1.81 A; A/B=29-516.
PDB; 2YXW; X-ray; 1.50 A; A/B=29-516.
PDB; 3NSC; X-ray; 1.50 A; A=29-516.
PDB; 3NSD; X-ray; 2.00 A; A=29-516.
PDB; 3NSF; X-ray; 2.00 A; A=29-516.
PDB; 3NSY; X-ray; 2.10 A; A=29-516.
PDB; 3NT0; X-ray; 1.80 A; A=29-516.
PDB; 3OD3; X-ray; 1.10 A; A=29-516.
PDB; 3PAU; X-ray; 2.00 A; A=29-516.
PDB; 3PAV; X-ray; 1.45 A; A=29-516.
PDB; 3QQX; X-ray; 1.50 A; A=29-516.
PDB; 3UAA; X-ray; 1.70 A; A=29-516.
PDB; 3UAB; X-ray; 1.30 A; A=29-516.
PDB; 3UAC; X-ray; 1.30 A; A=29-516.
PDB; 3UAD; X-ray; 1.10 A; A=29-516.
PDB; 3UAE; X-ray; 1.30 A; A=29-516.
PDB; 4E9Q; X-ray; 1.30 A; A=29-516.
PDB; 4E9R; X-ray; 1.30 A; A=29-516.
PDB; 4E9S; X-ray; 1.06 A; A=29-516.
PDB; 4E9T; X-ray; 1.30 A; A=29-516.
PDB; 4EF3; X-ray; 1.90 A; A=29-516.
PDB; 4HAK; X-ray; 1.40 A; A=29-516.
PDB; 4HAL; X-ray; 1.40 A; A=29-516.
PDB; 4NER; X-ray; 1.60 A; A=29-516.
PDB; 5B7E; X-ray; 1.42 A; A=1-516.
PDB; 5B7F; X-ray; 1.45 A; A=29-516.
PDB; 5B7M; X-ray; 1.80 A; A/B/C=29-516.
PDB; 5GNO; X-ray; 1.45 A; A=29-516.
PDBsum; 1KV7; -.
PDBsum; 1N68; -.
PDBsum; 1PF3; -.
PDBsum; 2FQD; -.
PDBsum; 2FQE; -.
PDBsum; 2FQF; -.
PDBsum; 2FQG; -.
PDBsum; 2YXV; -.
PDBsum; 2YXW; -.
PDBsum; 3NSC; -.
PDBsum; 3NSD; -.
PDBsum; 3NSF; -.
PDBsum; 3NSY; -.
PDBsum; 3NT0; -.
PDBsum; 3OD3; -.
PDBsum; 3PAU; -.
PDBsum; 3PAV; -.
PDBsum; 3QQX; -.
PDBsum; 3UAA; -.
PDBsum; 3UAB; -.
PDBsum; 3UAC; -.
PDBsum; 3UAD; -.
PDBsum; 3UAE; -.
PDBsum; 4E9Q; -.
PDBsum; 4E9R; -.
PDBsum; 4E9S; -.
PDBsum; 4E9T; -.
PDBsum; 4EF3; -.
PDBsum; 4HAK; -.
PDBsum; 4HAL; -.
PDBsum; 4NER; -.
PDBsum; 5B7E; -.
PDBsum; 5B7F; -.
PDBsum; 5B7M; -.
PDBsum; 5GNO; -.
ProteinModelPortal; P36649; -.
SMR; P36649; -.
BioGrid; 4261957; 12.
DIP; DIP-11178N; -.
IntAct; P36649; 5.
STRING; 316385.ECDH10B_0103; -.
TCDB; 1.B.76.1.8; the copper resistance putative porin (copb) family.
PaxDb; P36649; -.
PRIDE; P36649; -.
EnsemblBacteria; AAC73234; AAC73234; b0123.
EnsemblBacteria; BAB96698; BAB96698; BAB96698.
GeneID; 947736; -.
KEGG; ecj:JW0119; -.
KEGG; eco:b0123; -.
PATRIC; fig|1411691.4.peg.2159; -.
EchoBASE; EB2223; -.
EcoGene; EG12318; cueO.
eggNOG; ENOG4105E3B; Bacteria.
eggNOG; COG2132; LUCA.
HOGENOM; HOG000096435; -.
InParanoid; P36649; -.
KO; K14588; -.
PhylomeDB; P36649; -.
BioCyc; EcoCyc:EG12318-MONOMER; -.
BioCyc; MetaCyc:EG12318-MONOMER; -.
EvolutionaryTrace; P36649; -.
PRO; PR:P36649; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
GO; GO:0005507; F:copper ion binding; IDA:EcoCyc.
GO; GO:0004322; F:ferroxidase activity; IDA:EcoCyc.
GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IDA:EcoCyc.
GO; GO:0016722; F:oxidoreductase activity, oxidizing metal ions; IDA:EcoliWiki.
GO; GO:0016724; F:oxidoreductase activity, oxidizing metal ions, oxygen as acceptor; IDA:EcoCyc.
GO; GO:0010273; P:detoxification of copper ion; IDA:EcoCyc.
GO; GO:0046688; P:response to copper ion; IMP:EcoCyc.
Gene3D; 2.60.40.420; -; 3.
InterPro; IPR001117; Cu-oxidase.
InterPro; IPR011706; Cu-oxidase_2.
InterPro; IPR011707; Cu-oxidase_3.
InterPro; IPR002355; Cu_oxidase_Cu_BS.
InterPro; IPR008972; Cupredoxin.
InterPro; IPR006311; TAT_signal.
Pfam; PF00394; Cu-oxidase; 1.
Pfam; PF07731; Cu-oxidase_2; 1.
Pfam; PF07732; Cu-oxidase_3; 1.
SUPFAM; SSF49503; SSF49503; 4.
PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PROSITE; PS51318; TAT; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Copper; Direct protein sequencing;
Metal-binding; Oxidoreductase; Periplasm; Reference proteome; Repeat;
Signal.
SIGNAL 1 28 Tat-type signal. {ECO:0000255|PROSITE-
ProRule:PRU00648,
ECO:0000269|PubMed:9298646}.
CHAIN 29 516 Blue copper oxidase CueO.
/FTId=PRO_0000002951.
DOMAIN 67 163 Plastocyanin-like 1.
DOMAIN 164 410 Plastocyanin-like 2.
DOMAIN 411 516 Plastocyanin-like 3.
COMPBIAS 355 400 Met-rich.
METAL 101 101 Copper 1; type 2.
METAL 103 103 Copper 2; type 3.
METAL 141 141 Copper 2; type 3.
METAL 143 143 Copper 3; type 3.
METAL 443 443 Copper 4; type 1.
METAL 446 446 Copper 1; type 2.
METAL 448 448 Copper 3; type 3.
METAL 499 499 Copper 3; type 3.
METAL 500 500 Copper 4; type 1.
METAL 501 501 Copper 2; type 3.
METAL 505 505 Copper 4; type 1.
METAL 510 510 Copper 4; type 1.
MUTAGEN 500 501 CH->SR: Residual activity and loss of
resistance to copper.
{ECO:0000269|PubMed:11527384}.
STRAND 47 59 {ECO:0000244|PDB:4E9S}.
STRAND 62 74 {ECO:0000244|PDB:4E9S}.
STRAND 77 81 {ECO:0000244|PDB:4E9S}.
STRAND 85 92 {ECO:0000244|PDB:4E9S}.
STRAND 94 96 {ECO:0000244|PDB:4E9S}.
STRAND 101 103 {ECO:0000244|PDB:4E9S}.
HELIX 109 111 {ECO:0000244|PDB:4E9S}.
STRAND 124 130 {ECO:0000244|PDB:4E9S}.
STRAND 135 141 {ECO:0000244|PDB:4E9S}.
TURN 145 147 {ECO:0000244|PDB:4E9S}.
HELIX 148 153 {ECO:0000244|PDB:4E9S}.
STRAND 158 163 {ECO:0000244|PDB:4E9S}.
HELIX 165 169 {ECO:0000244|PDB:4E9S}.
TURN 177 179 {ECO:0000244|PDB:4E9S}.
STRAND 180 188 {ECO:0000244|PDB:4E9S}.
STRAND 194 196 {ECO:0000244|PDB:4E9S}.
HELIX 202 207 {ECO:0000244|PDB:4E9S}.
STRAND 212 216 {ECO:0000244|PDB:4E9S}.
STRAND 219 221 {ECO:0000244|PDB:4E9S}.
STRAND 223 237 {ECO:0000244|PDB:4E9S}.
STRAND 244 248 {ECO:0000244|PDB:4E9S}.
STRAND 254 259 {ECO:0000244|PDB:4E9S}.
STRAND 262 271 {ECO:0000244|PDB:4E9S}.
STRAND 273 275 {ECO:0000244|PDB:4E9S}.
STRAND 280 287 {ECO:0000244|PDB:4E9S}.
STRAND 293 297 {ECO:0000244|PDB:4E9S}.
TURN 303 306 {ECO:0000244|PDB:4E9S}.
TURN 308 311 {ECO:0000244|PDB:4E9S}.
STRAND 314 325 {ECO:0000244|PDB:4E9S}.
STRAND 348 355 {ECO:0000244|PDB:4E9S}.
HELIX 357 371 {ECO:0000244|PDB:4E9S}.
HELIX 372 376 {ECO:0000244|PDB:4E9S}.
HELIX 381 384 {ECO:0000244|PDB:3OD3}.
HELIX 400 402 {ECO:0000244|PDB:4E9S}.
HELIX 404 406 {ECO:0000244|PDB:4E9S}.
STRAND 408 410 {ECO:0000244|PDB:4E9S}.
STRAND 421 424 {ECO:0000244|PDB:4E9S}.
STRAND 426 428 {ECO:0000244|PDB:4E9S}.
STRAND 430 435 {ECO:0000244|PDB:4E9S}.
STRAND 443 447 {ECO:0000244|PDB:4E9S}.
STRAND 452 457 {ECO:0000244|PDB:4E9S}.
HELIX 464 466 {ECO:0000244|PDB:4E9S}.
STRAND 470 484 {ECO:0000244|PDB:4E9S}.
HELIX 492 494 {ECO:0000244|PDB:4E9S}.
STRAND 496 502 {ECO:0000244|PDB:4E9S}.
HELIX 503 507 {ECO:0000244|PDB:4E9S}.
STRAND 511 516 {ECO:0000244|PDB:4E9S}.
SEQUENCE 516 AA; 56556 MW; 37D96B1C331CF30B CRC64;
MQRRDFLKYS VALGVASALP LWSRAVFAAE RPTLPIPDLL TTDARNRIQL TIGAGQSTFG
GKTATTWGYN GNLLGPAVKL QRGKAVTVDI YNQLTEETTL HWHGLEVPGE VDGGPQGIIP
PGGKRSVTLN VDQPAATCWF HPHQHGKTGR QVAMGLAGLV VIEDDEILKL MLPKQWGIDD
VPVIVQDKKF SADGQIDYQL DVMTAAVGWF GDTLLTNGAI YPQHAAPRGW LRLRLLNGCN
ARSLNFATSD NRPLYVIASD GGLLPEPVKV SELPVLMGER FEVLVEVNDN KPFDLVTLPV
SQMGMAIAPF DKPHPVMRIQ PIAISASGAL PDTLSSLPAL PSLEGLTVRK LQLSMDPMLD
MMGMQMLMEK YGDQAMAGMD HSQMMGHMGH GNMNHMNHGG KFDFHHANKI NGQAFDMNKP
MFAAAKGQYE RWVISGVGDM MLHPFHIHGT QFRILSENGK PPAAHRAGWK DTVKVEGNVS
EVLVKFNHDA PKEHAYMAHC HLLEHEDTGM MLGFTV


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