RegulonDB

Gene
Name:	cueO
Synonym(s):	ECK0122, EG12318, b0123, yacK
Genome position(nucleotides):	137083 --> 138633 Genome Browser
Strand:	forward
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	54.67
External database links:

ASAP:	ABE-0000430
ECHOBASE:	EB2223
OU-MICROARRAY:	b0123
PortEco:	cueO
STRING:	511145.b0123
COLOMBOS:	cueO

Gene

Name:

cueO

Synonym(s):

ECK0122, EG12318, b0123, yacK

Genome position(nucleotides):

137083 --> 138633 Genome Browser

Strand:

forward

Sequence:

Get nucleotide sequence FastaFormat

GC content %:

54.67

External database links:

ASAP:

ECHOBASE:

OU-MICROARRAY:

PortEco:

STRING:

COLOMBOS:

Type

Positions

Sequence

500 -> 501

304 -> 304

439 -> 439

441 -> 441

67 -> 163

WGYNGNLLGPAVKLQRGKAVTVDIYNQLTEETTLHWHGLEVPGEVDGGPQGIIPPGGKRSVTLNVDQPAATCWFHPHQHGKTGRQVAMGLAGLVVIE

Type

Positions

Sequence

500 -> 501

304 -> 304

439 -> 439

441 -> 441

67 -> 163

WGYNGNLLGPAVKLQRGKAVTVDIYNQLTEETTLHWHGLEVPGEVDGGPQGIIPPGGKRSVTLNVDQPAATCWFHPHQHGKTGRQVAMGLAGLVVIE

164 -> 410

DDEILKLMLPKQWGIDDVPVIVQDKKFSADGQIDYQLDVMTAAVGWFGDTLLTNGAIYPQHAAPRGWLRLRLLNGCNARSLNFATSDNRPLYVIASDGGLLPEPVKVSELPVLMGERFEVLVEVNDNKPFDLVTLPVSQMGMAIAPFDKPHPVMRIQPIAISASGALPDTLSSLPALPSLEGLTVRKLQLSMDPMLDMMGMQMLMEKYGDQAMAGMDHSQMMGHMGHGNMNHMNHGGKFDFHHANKI

355 -> 370

MDPMLDMMGMQMLMEK

360 -> 360

402 -> 516

FDFHHANKINGQAFDMNKPMFAAAKGQYERWVISGVGDMMLHPFHIHGTQFRILSENGKPPAAHRAGWKDTVKVEGNVSEVLVKFNHDAPKEHAYMAHCHLLEHEDTGMMLGFTV

1 -> 28

MQRRDFLKYSVALGVASALPLWSRAVFA

29 -> 516

AERPTLPIPDLLTTDARNRIQLTIGAGQSTFGGKTATTWGYNGNLLGPAVKLQRGKAVTVDIYNQLTEETTLHWHGLEVPGEVDGGPQGIIPPGGKRSVTLNVDQPAATCWFHPHQHGKTGRQVAMGLAGLVVIEDDEILKLMLPKQWGIDDVPVIVQDKKFSADGQIDYQLDVMTAAVGWFGDTLLTNGAIYPQHAAPRGWLRLRLLNGCNARSLNFATSDNRPLYVIASDGGLLPEPVKVSELPVLMGERFEVLVEVNDNKPFDLVTLPVSQMGMAIAPFDKPHPVMRIQPIAISASGALPDTLSSLPALPSLEGLTVRKLQLSMDPMLDMMGMQMLMEKYGDQAMAGMDHSQMMGHMGHGNMNHMNHGGKFDFHHANKINGQAFDMNKPMFAAAKGQYERWVISGVGDMMLHPFHIHGTQFRILSENGKPPAAHRAGWKDTVKVEGNVSEVLVKFNHDAPKEHAYMAHCHLLEHEDTGMMLGFTV

227 -> 292

PRGWLRLRLLNGCNARSLNFATSDNRPLYVIASDGGLLPEPVKVSELPVLMGERFEVLVEVNDNKP

411 -> 516

NGQAFDMNKPMFAAAKGQYERWVISGVGDMMLHPFHIHGTQFRILSENGKPPAAHRAGWKDTVKVEGNVSEVLVKFNHDAPKEHAYMAHCHLLEHEDTGMMLGFTV

55 -> 165

GQSTFGGKTATTWGYNGNLLGPAVKLQRGKAVTVDIYNQLTEETTLHWHGLEVPGEVDGGPQGIIPPGGKRSVTLNVDQPAATCWFHPHQHGKTGRQVAMGLAGLVVIEDD

Multifun Terms (GenProtEC)

1 - metabolism

5 - cell processes --> 5.5 - adaptations --> 5.5.6 - other (mechanical, nutritional, oxidative stress)

5 - cell processes --> 5.6 - protection --> 5.6.2 - detoxification

Gene Ontology Terms (GO)

cellular_component

GO:0030288 - outer membrane-bounded periplasmic space
GO:0042597 - periplasmic space

molecular_function

GO:0005507 - copper ion binding
GO:0046872 - metal ion binding
GO:0016491 - oxidoreductase activity
GO:0004322 - ferroxidase activity
GO:0016724 - oxidoreductase activity, oxidizing metal ions, oxygen as acceptor
GO:0016722 - oxidoreductase activity, oxidizing metal ions
GO:0016682 - oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor

biological_process

GO:0046688 - response to copper ion
GO:0055114 - oxidation-reduction process
GO:0010273 - detoxification of copper ion

Transcriptional Regulation
	Display Regulation
Activated by:	CueR

Transcriptional Regulation

Display Regulation

Activated by:

CueR

Regulation by small RNA
	Display Regulation
small RNA	ryhB

Regulation by small RNA

Display Regulation

small RNA

ryhB

Type	Name	Post Left	Strand	Notes	Evidence (Confirmed, Strong, Weak)	References
promoter	TSS_263 (cluster)	137048	forward	For this promoter, there is a cluster of 2 transcription start sites,in the interval 137048 to 137049, where the highest frequency is at position 137048. The most upstream position of this cluster is assigned as TSS position in the promoter. Read more >	[RS-EPT-CBR]	[16]
promoter	TSS_264	137069	forward	nd	[RS-EPT-CBR]	[16]
promoter	TSS_265	137630	reverse	nd	[RS-EPT-CBR]	[16]

Type

Name

Post Left

Post Right

Strand

Notes

Evidence (Confirmed, Strong, Weak)

References

promoter

TSS_263 (cluster)

137048

forward

For this promoter, there
Read more >

[RS-EPT-CBR]

[16]

promoter

TSS_264

137069

forward

[RS-EPT-CBR]

[16]

promoter

TSS_265

137630

reverse

[RS-EPT-CBR]

[16]

Evidence
[RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

Evidence

[RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

Reference(s)
[1] Akter M., Inoue C., Komori H., Matsuda N., Sakurai T., Kataoka K., Higuchi Y., Shibata N., 2016, Biochemical, spectroscopic and X-ray structural analysis of deuterated multicopper oxidase CueO prepared from a new expression construct for neutron crystallography., Acta Crystallogr F Struct Biol Commun 72(Pt 10):788-794
[2] Graubner W., Schierhorn A., Bruser T., 2007, DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone., J Biol Chem 282(10):7116-24
[3] Iwaki M., Kataoka K., Kajino T., Sugiyama R., Morishita H., Sakurai T., 2010, ATR-FTIR study of the protonation states of the Glu residue in the multicopper oxidases, CueO and bilirubin oxidase., FEBS Lett 584(18):4027-31
[4] Kajikawa T., Kataoka K., Sakurai T., 2012, Modifications on the hydrogen bond network by mutations of Escherichia coli copper efflux oxidase affect the process of proton transfer to dioxygen leading to alterations of enzymatic activities., Biochem Biophys Res Commun 422(1):152-6
[5] Kataoka K., Hirota S., Maeda Y., Kogi H., Shinohara N., Sekimoto M., Sakurai T., 2011, Enhancement of laccase activity through the construction and breakdown of a hydrogen bond at the type I copper center in Escherichia coli CueO and the deletion mutant Δα5-7 CueO., Biochemistry 50(4):558-65
[6] Kataoka K., Kogi H., Tsujimura S., Sakurai T., 2013, Modifications of laccase activities of copper efflux oxidase, CueO by synergistic mutations in the first and second coordination spheres of the type I copper center., Biochem Biophys Res Commun 431(3):393-7
[7] Kataoka K., Sugiyama R., Hirota S., Inoue M., Urata K., Minagawa Y., Seo D., Sakurai T., 2009, Four-electron reduction of dioxygen by a multicopper oxidase, CueO, and roles of Asp112 and Glu506 located adjacent to the trinuclear copper center., J Biol Chem 284(21):14405-13
[8] Komori H., Kajikawa T., Kataoka K., Higuchi Y., Sakurai T., 2013, Crystal structure of the CueO mutants at Glu506, the key amino acid located in the proton transfer pathway for dioxygen reduction., Biochem Biophys Res Commun 438(4):686-90
[9] Lee SM., Grass G., Rensing C., Barrett SR., Yates CJ., Stoyanov JV., Brown NL., 2002, The Pco proteins are involved in periplasmic copper handling in Escherichia coli., Biochem Biophys Res Commun 295(3):616-20
[10] Li X., Wei Z., Zhang M., Peng X., Yu G., Teng M., Gong W., 2007, Crystal structures of E. coli laccase CueO at different copper concentrations., Biochem Biophys Res Commun 354(1):21-6
[11] Merlin C., McAteer S., Masters M., 2002, Tools for characterization of Escherichia coli genes of unknown function., J Bacteriol 184(16):4573-81
[12] Sakurai T., Yamamoto M., Ikeno S., Kataoka K., 2017, Amino acids located in the outer-sphere of the trinuclear copper center in a multicopper oxidase, CueO as the putative electron donor in the four-electron reduction of dioxygen., Biochim Biophys Acta Proteins Proteom 1865(8):997-1003
[13] Sana B., Chee SMQ., Wongsantichon J., Raghavan S., Robinson RC., Ghadessy FJ., 2019, Development and structural characterization of an engineered multi-copper oxidase reporter of protein-protein interactions., J Biol Chem
[14] Ueki Y., Inoue M., Kurose S., Kataoka K., Sakurai T., 2006, Mutations at Asp112 adjacent to the trinuclear Cu center in CueO as the proton donor in the four-electron reduction of dioxygen., FEBS Lett 580(17):4069-72
[15] Xu Z., Wang P., Wang H., Yu ZH., Au-Yeung HY., Hirayama T., Sun H., Yan A., 2019, Zinc excess increases cellular demand for iron and decreases tolerance to copper in Escherichia coli., J Biol Chem 294(45):16978-16991
[16] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

Reference(s)

[1] Akter M., Inoue C., Komori H., Matsuda N., Sakurai T., Kataoka K., Higuchi Y., Shibata N., 2016, Biochemical, spectroscopic and X-ray structural analysis of deuterated multicopper oxidase CueO prepared from a new expression construct for neutron crystallography., Acta Crystallogr F Struct Biol Commun 72(Pt 10):788-794

[2] Graubner W., Schierhorn A., Bruser T., 2007, DnaK plays a pivotal role in Tat targeting of CueO and functions beside SlyD as a general Tat signal binding chaperone., J Biol Chem 282(10):7116-24

[3] Iwaki M., Kataoka K., Kajino T., Sugiyama R., Morishita H., Sakurai T., 2010, ATR-FTIR study of the protonation states of the Glu residue in the multicopper oxidases, CueO and bilirubin oxidase., FEBS Lett 584(18):4027-31

[4] Kajikawa T., Kataoka K., Sakurai T., 2012, Modifications on the hydrogen bond network by mutations of Escherichia coli copper efflux oxidase affect the process of proton transfer to dioxygen leading to alterations of enzymatic activities., Biochem Biophys Res Commun 422(1):152-6

[5] Kataoka K., Hirota S., Maeda Y., Kogi H., Shinohara N., Sekimoto M., Sakurai T., 2011, Enhancement of laccase activity through the construction and breakdown of a hydrogen bond at the type I copper center in Escherichia coli CueO and the deletion mutant Δα5-7 CueO., Biochemistry 50(4):558-65

[6] Kataoka K., Kogi H., Tsujimura S., Sakurai T., 2013, Modifications of laccase activities of copper efflux oxidase, CueO by synergistic mutations in the first and second coordination spheres of the type I copper center., Biochem Biophys Res Commun 431(3):393-7

[7] Kataoka K., Sugiyama R., Hirota S., Inoue M., Urata K., Minagawa Y., Seo D., Sakurai T., 2009, Four-electron reduction of dioxygen by a multicopper oxidase, CueO, and roles of Asp112 and Glu506 located adjacent to the trinuclear copper center., J Biol Chem 284(21):14405-13

[8] Komori H., Kajikawa T., Kataoka K., Higuchi Y., Sakurai T., 2013, Crystal structure of the CueO mutants at Glu506, the key amino acid located in the proton transfer pathway for dioxygen reduction., Biochem Biophys Res Commun 438(4):686-90

[9] Lee SM., Grass G., Rensing C., Barrett SR., Yates CJ., Stoyanov JV., Brown NL., 2002, The Pco proteins are involved in periplasmic copper handling in Escherichia coli., Biochem Biophys Res Commun 295(3):616-20

[10] Li X., Wei Z., Zhang M., Peng X., Yu G., Teng M., Gong W., 2007, Crystal structures of E. coli laccase CueO at different copper concentrations., Biochem Biophys Res Commun 354(1):21-6

[11] Merlin C., McAteer S., Masters M., 2002, Tools for characterization of Escherichia coli genes of unknown function., J Bacteriol 184(16):4573-81

[12] Sakurai T., Yamamoto M., Ikeno S., Kataoka K., 2017, Amino acids located in the outer-sphere of the trinuclear copper center in a multicopper oxidase, CueO as the putative electron donor in the four-electron reduction of dioxygen., Biochim Biophys Acta Proteins Proteom 1865(8):997-1003

[13] Sana B., Chee SMQ., Wongsantichon J., Raghavan S., Robinson RC., Ghadessy FJ., 2019, Development and structural characterization of an engineered multi-copper oxidase reporter of protein-protein interactions., J Biol Chem

[14] Ueki Y., Inoue M., Kurose S., Kataoka K., Sakurai T., 2006, Mutations at Asp112 adjacent to the trinuclear Cu center in CueO as the proton donor in the four-electron reduction of dioxygen., FEBS Lett 580(17):4069-72

[15] Xu Z., Wang P., Wang H., Yu ZH., Au-Yeung HY., Hirayama T., Sun H., Yan A., 2019, Zinc excess increases cellular demand for iron and decreases tolerance to copper in Escherichia coli., J Biol Chem 294(45):16978-16991

[16] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.