[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1093/nar/22.9.1637; PubMed=8202364 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] 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 277:1453-1474(1997).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1002/(SICI)1522-2683(19990801)20:11<2181::AID-ELPS2181>3.3.CO;2-H; PubMed=10493123 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1128/JB.183.6.2145-2147.2001; PubMed=11222619 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1074/jbc.M104122200; PubMed=11399769 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1074/jbc.M006508200; PubMed=10915804 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1128/JB.183.16.4866-4875.2001; PubMed=11466290 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1006/bbrc.2001.5474; PubMed=11527384 [NCBI, ExPASy, EBI, Israel, Japan] 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]	X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS). STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1073/pnas.052710499; PubMed=11867755 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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: Binds 4 copper ions per monomer.
SUBUNIT: Monomer (Probable).
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: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
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.
SIMILARITY: Contains 3 plastocyanin-like domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U00096; AAC73234.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAB96698.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C64735; C64735.

RefSeq

AP_000784.1; -.
NP_414665.1; -.

3D structure databases

PDB

1KV7; X-ray; 1.40 A; A=29-516.	[ExPASy / RCSB / EBI]
1N68; X-ray; 1.70 A; A=29-516.	[ExPASy / RCSB / EBI]
1PF3; X-ray; 1.50 A; A=29-516.	[ExPASy / RCSB / EBI]
2FQD; X-ray; 2.40 A; A=29-516.	[ExPASy / RCSB / EBI]
2FQE; X-ray; 1.92 A; A=29-516.	[ExPASy / RCSB / EBI]
2FQF; X-ray; 2.00 A; A=29-516.	[ExPASy / RCSB / EBI]
2FQG; X-ray; 2.30 A; A=29-516.	[ExPASy / RCSB / EBI]
2YXV; X-ray; 1.81 A; A/B=29-516.	[ExPASy / RCSB / EBI]
2YXW; X-ray; 1.50 A; A/B=29-516.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1KV7; -.
1N68; -.
1PF3; -.
2FQD; -.
2FQE; -.
2FQF; -.
2FQG; -.
2YXV; -.
2YXW; -.

ModBase

P36649.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12318-MON; -.
MetaCyc:EG12318-MON; -.

Organism-specific databases

EchoBASE

EB2223; -.

EcoGene

EG12318; cueO.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0016491;	Molecular function: oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR011706; Cu-oxidase_2.
IPR011707; Cu-oxidase_3.
IPR002355; Cu_oxidase_Cu_BS.
IPR008972; Cupredoxin.
IPR006311; Tat.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.420; Cupredoxin; 3.

Pfam

PF07731; Cu-oxidase_2; 1.
PF07732; Cu-oxidase_3; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01409; TAT_signal_seq; 1.

PROSITE

PS00080; MULTICOPPER_OXIDASE2; 1.
PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P36649.

Genome annotation databases

GeneID

947736; -.

GenomeReviews

U00096_GR; b0123.
AP009048_GR; JW0119.

KEGG

ecj:JW0119; -.
eco:b0123; -.

Phylogenomic databases

HOGENOM

P36649; -.

Genome annotation databases

CMR

P36649; b0123.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Copper; Direct protein sequencing; Metal-binding; Oxidoreductase; Periplasm; Repeat; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 28`	`28`	`Tat-type signal.`
`CHAIN`	`29 516`	`488`	`Blue copper oxidase cueO.`	`PRO_0000002951`
`DOMAIN`	`67 163`	`97`	`Plastocyanin-like 1.`
`DOMAIN`	`164 410`	`247`	`Plastocyanin-like 2.`
`DOMAIN`	`411 516`	`106`	`Plastocyanin-like 3.`
`COMPBIAS`	`355 400`	`46`	`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.`
`STRAND`	`46 59`	`14`
`STRAND`	`62 74`	`13`
`STRAND`	`77 81`	`5`
`STRAND`	`85 92`	`8`
`STRAND`	`94 96`	`3`
`STRAND`	`101 103`	`3`
`HELIX`	`109 111`	`3`
`STRAND`	`124 130`	`7`
`STRAND`	`135 141`	`7`
`TURN`	`145 147`	`3`
`HELIX`	`148 153`	`6`
`STRAND`	`158 163`	`6`
`HELIX`	`165 169`	`5`
`TURN`	`177 179`	`3`
`STRAND`	`180 188`	`9`
`STRAND`	`194 196`	`3`
`HELIX`	`202 207`	`6`
`STRAND`	`212 216`	`5`
`STRAND`	`219 221`	`3`
`STRAND`	`223 237`	`15`
`STRAND`	`244 248`	`5`
`STRAND`	`254 259`	`6`
`STRAND`	`262 271`	`10`
`STRAND`	`273 275`	`3`
`STRAND`	`280 287`	`8`
`STRAND`	`293 297`	`5`
`TURN`	`303 306`	`4`
`TURN`	`308 311`	`4`
`STRAND`	`314 325`	`12`
`STRAND`	`347 355`	`9`
`HELIX`	`357 371`	`15`
`HELIX`	`372 376`	`5`
`HELIX`	`404 406`	`3`
`STRAND`	`408 410`	`3`
`STRAND`	`421 423`	`3`
`STRAND`	`426 428`	`3`
`STRAND`	`430 435`	`6`
`STRAND`	`443 447`	`5`
`STRAND`	`452 457`	`6`
`HELIX`	`464 466`	`3`
`STRAND`	`467 484`	`18`
`HELIX`	`492 494`	`3`
`STRAND`	`496 502`	`7`
`HELIX`	`503 507`	`5`
`STRAND`	`511 515`	`5`

Sequence information

Length: 516 AA [This is the length of the unprocessed precursor]

Molecular weight: 56556 Da [This is the MW of the unprocessed precursor]

CRC64: 37D96B1C331CF30B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQRRDFLKYS VALGVASALP LWSRAVFAAE RPTLPIPDLL TTDARNRIQL TIGAGQSTFG 

        70         80         90        100        110        120 
GKTATTWGYN GNLLGPAVKL QRGKAVTVDI YNQLTEETTL HWHGLEVPGE VDGGPQGIIP 

       130        140        150        160        170        180 
PGGKRSVTLN VDQPAATCWF HPHQHGKTGR QVAMGLAGLV VIEDDEILKL MLPKQWGIDD 

       190        200        210        220        230        240 
VPVIVQDKKF SADGQIDYQL DVMTAAVGWF GDTLLTNGAI YPQHAAPRGW LRLRLLNGCN 

       250        260        270        280        290        300 
ARSLNFATSD NRPLYVIASD GGLLPEPVKV SELPVLMGER FEVLVEVNDN KPFDLVTLPV 

       310        320        330        340        350        360 
SQMGMAIAPF DKPHPVMRIQ PIAISASGAL PDTLSSLPAL PSLEGLTVRK LQLSMDPMLD 

       370        380        390        400        410        420 
MMGMQMLMEK YGDQAMAGMD HSQMMGHMGH GNMNHMNHGG KFDFHHANKI NGQAFDMNKP 

       430        440        450        460        470        480 
MFAAAKGQYE RWVISGVGDM MLHPFHIHGT QFRILSENGK PPAAHRAGWK DTVKVEGNVS 

       490        500        510 
EVLVKFNHDA PKEHAYMAHC HLLEHEDTGM MLGFTV

P36649 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools