Reviewed, UniProtKB/Swiss-Prot P36649 (CUEO_ECOLI)

Names and origin

Protein names

Recommended name:
    Blue copper oxidase cueO
Alternative name(s):
    Copper efflux oxidase

Gene names

Name:	cueO
Synonyms:	yacK
Ordered Locus Names:	b0123, JW0119

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	516 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably involved in periplasmic detoxification of copper by oxidizing Cu+ to Cu2+ 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. Ref.6 Ref.7
Cofactor	Binds 4 copper ions per monomer.
Subunit structure	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.
Post-translational modification	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.
Sequence similarities	Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Tat-type signal Ref.4

Chain

29 – 516

488

Blue copper oxidase cueO

PRO_0000002951

Regions

Domain

67 – 163

97

Plastocyanin-like 1

Domain

164 – 410

247

Plastocyanin-like 2

Domain

411 – 516

106

Plastocyanin-like 3

Compositional bias

355 – 400

46

Met-rich

Sites

Metal binding

101

1

Copper 1; type 2

Metal binding

103

1

Copper 2; type 3

Metal binding

141

1

Copper 2; type 3

Metal binding

143

1

Copper 3; type 3

Metal binding

443

1

Copper 4; type 1

Metal binding

446

1

Copper 1; type 2

Metal binding

448

1

Copper 3; type 3

Metal binding

499

1

Copper 3; type 3

Metal binding

500

1

Copper 4; type 1

Metal binding

501

1

Copper 2; type 3

Metal binding

505

1

Copper 4; type 1

Metal binding

510

1

Copper 4; type 1

Experimental info

Mutagenesis

500 – 501

2

CH → SR: Residual activity and loss of resistance to copper. Ref.10

Secondary structure

1

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516

Helix Strand Turn

Details...

Beta strand

46 – 59

14

Beta strand

62 – 74

13

Beta strand

77 – 81

5

Beta strand

85 – 92

8

Beta strand

94 – 96

3

Beta strand

101 – 103

3

Helix

109 – 111

3

Beta strand

124 – 130

7

Beta strand

135 – 141

7

Turn

145 – 147

3

Helix

148 – 153

6

Beta strand

158 – 163

6

Helix

165 – 169

5

Turn

177 – 179

3

Beta strand

180 – 188

9

Beta strand

194 – 196

3

Helix

202 – 207

6

Beta strand

212 – 216

5

Beta strand

219 – 221

3

Beta strand

223 – 237

15

Beta strand

244 – 248

5

Beta strand

254 – 259

6

Beta strand

262 – 271

10

Beta strand

273 – 275

3

Beta strand

280 – 287

8

Beta strand

293 – 297

5

Turn

303 – 306

4

Turn

308 – 311

4

Beta strand

314 – 325

12

Beta strand

347 – 355

9

Helix

357 – 371

15

Helix

372 – 376

5

Helix

404 – 406

3

Beta strand

408 – 410

3

Beta strand

421 – 423

3

Beta strand

426 – 428

3

Beta strand

430 – 435

6

Beta strand

443 – 447

5

Beta strand

452 – 457

6

Helix

464 – 466

3

Beta strand

467 – 484

18

Helix

492 – 494

3

Beta strand

496 – 502

7

Helix

503 – 507

5

Beta strand

511 – 515

5

Sequences

	Sequence		Length	Mass (Da)
	P36649-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 37D96B1C331CF30B	FASTA	516	56,556
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed: 8202364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-40. Strain: K12 / EMG2.
[5]	"Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography." Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B. Electrophoresis 20:2181-2195(1999) [PubMed: 10493123] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[6]	"Genes involved in copper homeostasis in Escherichia coli." Grass G., Rensing C. J. Bacteriol. 183:2145-2147(2001) [PubMed: 11222619] [Abstract] Cited for: POSSIBLE FUNCTION IN COPPER HOMEOSTASIS.
[7]	"The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli." Outten F.W., Huffman D.L., Hale J.A., O'Halloran T.V. J. Biol. Chem. 276:30670-30677(2001) [PubMed: 11399769] [Abstract] Cited for: POSSIBLE FUNCTION IN COPPER HOMEOSTASIS. Strain: K12.
[8]	"Transcriptional activation of an Escherichia coli copper efflux regulon by the chromosomal merR homologue, cueR." Outten F.W., Outten C.E., Hale J.A., O'Halloran T.V. J. Biol. Chem. 275:31024-31029(2000) [PubMed: 10915804] [Abstract] Cited for: CHARACTERIZATION. Strain: K12 / DH5-alpha.
[9]	"Oxidation of phenolate siderophores by the multicopper oxidase encoded by the Escherichia coli yacK gene." Kim C., Lorenz W.W., Hoopes J.T., Dean J.F.D. J. Bacteriol. 183:4866-4875(2001) [PubMed: 11466290] [Abstract] Cited for: CHARACTERIZATION. Strain: K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222.
[10]	"CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli." Grass G., Rensing C. Biochem. Biophys. Res. Commun. 286:902-908(2001) [PubMed: 11527384] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF 500-CYS-HIS-501. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[11]	"Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli." Roberts S.A., Weichsel A., Grass G., Thakali K., Hazzard J.T., Tollin G., Rensing C., Montfort W.R. Proc. Natl. Acad. Sci. U.S.A. 99:2766-2771(2002) [PubMed: 11867755] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS). Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U00096 Genomic DNA. Translation: AAC73234.1.
AP009048 Genomic DNA. Translation: BAB96698.2.

PIR

C64735.

RefSeq

AP_000784.1.
NP_414665.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KV7	X-ray	1.40	A	29-516	[»]
1N68	X-ray	1.70	A	29-516	[»]
1PF3	X-ray	1.50	A	29-516	[»]
2FQD	X-ray	2.40	A	29-516	[»]
2FQE	X-ray	1.92	A	29-516	[»]
2FQF	X-ray	2.00	A	29-516	[»]
2FQG	X-ray	2.30	A	29-516	[»]
2YXV	X-ray	1.81	A/B	29-516	[»]
2YXW	X-ray	1.50	A/B	29-516	[»]

ModBase

Search...

Genome annotation databases

GeneID

947736.

GenomeReviews

Gene locus JW0119 in contig AP009048_GR.
Gene locus b0123 in contig U00096_GR.

KEGG

ecj:JW0119.
eco:b0123.

Organism-specific databases

EchoBASE

EB2223.

EcoGene

EG12318. cueO.

CMR

Search...

Phylogenomic databases

HOGENOM

P36649.

OMA

P36649. VAHKEVA.

Enzyme and pathway databases

BioCyc

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

Family and domain databases

InterPro

IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR006311. Tat.
IPR017909. Twin_arg_translocation_Tat.
[Graphical view]

Gene3D

G3DSA:2.60.40.420. Cupredoxin. 3 hits.

Pfam

PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01409. TAT_signal_seq. 1 hit.

PROSITE

PS00080. MULTICOPPER_OXIDASE2. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CUEO_ECOLI

Accession

Primary (citable) accession number: P36649
Secondary accession number(s): P75655, Q8KMZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)