Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

HTH-type transcriptional regulator CueR

Gene

cueR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates the transcription of the copA and cueO genes. It detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi112 – 1121Copper(1+)
Metal bindingi120 – 1201Copper(1+)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi4 – 2320H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cellular response to metal ion Source: GOC
  • positive regulation of transcription, DNA-templated Source: EcoCyc
  • transcription, DNA-templated Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Copper, DNA-binding, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G6263-MONOMER.
ECOL316407:JW0476-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional regulator CueR
Alternative name(s):
Copper efflux regulator
Copper export regulator
Gene namesi
Name:cueR
Synonyms:ybbI
Ordered Locus Names:b0487, JW0476
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13256. cueR.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1121C → S: Loss of sensitivity to copper. 2 Publications
Mutagenesisi120 – 1201C → S: Loss of sensitivity to copper. 2 Publications
Mutagenesisi129 – 1291C → S: No effect on response to copper. 2 Publications
Mutagenesisi130 – 1301C → S: No effect on response to copper. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 135135HTH-type transcriptional regulator CueRPRO_0000098111Add
BLAST

Proteomic databases

PaxDbiP0A9G4.
PRIDEiP0A9G4.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4259848. 11 interactions.
DIPiDIP-51206N.
IntActiP0A9G4. 4 interactions.
STRINGi511145.b0487.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 108Combined sources
Helixi14 – 229Combined sources
Helixi41 – 5515Combined sources
Helixi60 – 7112Combined sources
Turni73 – 764Combined sources
Helixi77 – 11034Combined sources
Beta strandi115 – 1184Combined sources
Helixi121 – 1266Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q05X-ray2.20A/B1-135[»]
1Q06X-ray2.07A/B1-135[»]
1Q07X-ray2.50A/B1-135[»]
4WLSX-ray2.10A/B1-128[»]
4WLWX-ray2.80A1-135[»]
ProteinModelPortaliP0A9G4.
SMRiP0A9G4. Positions 1-130.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9G4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6969HTH merR-typePROSITE-ProRule annotationAdd
BLAST

Domaini

It contains an N-terminal DNA binding region and a C-terminal metal binding region.

Sequence similaritiesi

Contains 1 HTH merR-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108Z6Z. Bacteria.
COG0789. LUCA.
HOGENOMiHOG000266076.
InParanoidiP0A9G4.
KOiK11923.
OMAiCPCAVAE.
OrthoDBiEOG6NKQXH.
PhylomeDBiP0A9G4.

Family and domain databases

InterProiIPR011789. CueR.
IPR009061. DNA-bd_dom_put.
IPR000551. MerR-type_HTH_dom.
[Graphical view]
PfamiPF13411. MerR_1. 1 hit.
[Graphical view]
PRINTSiPR00040. HTHMERR.
SMARTiSM00422. HTH_MERR. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 1 hit.
TIGRFAMsiTIGR02044. CueR. 1 hit.
PROSITEiPS00552. HTH_MERR_1. 1 hit.
PS50937. HTH_MERR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A9G4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNISDVAKIT GLTSKAIRFY EEKGLVTPPM RSENGYRTYT QQHLNELTLL
60 70 80 90 100
RQARQVGFNL EESGELVNLF NDPQRHSADV KRRTLEKVAE IERHIEELQS
110 120 130
MRDQLLALAN ACPGDDSADC PIIENLSGCC HHRAG
Length:135
Mass (Da):15,235
Last modified:July 19, 2005 - v1
Checksum:iA3AE39F9E3140862
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF318185 Genomic DNA. Translation: AAK06655.1.
U82664 Genomic DNA. Translation: AAB40241.1.
U00096 Genomic DNA. Translation: AAC73589.1.
AP009048 Genomic DNA. Translation: BAE76266.1.
PIRiF64779.
RefSeqiNP_415020.1. NC_000913.3.
WP_001026747.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73589; AAC73589; b0487.
BAE76266; BAE76266; BAE76266.
GeneIDi945332.
KEGGiecj:JW0476.
eco:b0487.
PATRICi32116133. VBIEscCol129921_0508.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF318185 Genomic DNA. Translation: AAK06655.1.
U82664 Genomic DNA. Translation: AAB40241.1.
U00096 Genomic DNA. Translation: AAC73589.1.
AP009048 Genomic DNA. Translation: BAE76266.1.
PIRiF64779.
RefSeqiNP_415020.1. NC_000913.3.
WP_001026747.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q05X-ray2.20A/B1-135[»]
1Q06X-ray2.07A/B1-135[»]
1Q07X-ray2.50A/B1-135[»]
4WLSX-ray2.10A/B1-128[»]
4WLWX-ray2.80A1-135[»]
ProteinModelPortaliP0A9G4.
SMRiP0A9G4. Positions 1-130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259848. 11 interactions.
DIPiDIP-51206N.
IntActiP0A9G4. 4 interactions.
STRINGi511145.b0487.

Proteomic databases

PaxDbiP0A9G4.
PRIDEiP0A9G4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73589; AAC73589; b0487.
BAE76266; BAE76266; BAE76266.
GeneIDi945332.
KEGGiecj:JW0476.
eco:b0487.
PATRICi32116133. VBIEscCol129921_0508.

Organism-specific databases

EchoBASEiEB3044.
EcoGeneiEG13256. cueR.

Phylogenomic databases

eggNOGiENOG4108Z6Z. Bacteria.
COG0789. LUCA.
HOGENOMiHOG000266076.
InParanoidiP0A9G4.
KOiK11923.
OMAiCPCAVAE.
OrthoDBiEOG6NKQXH.
PhylomeDBiP0A9G4.

Enzyme and pathway databases

BioCyciEcoCyc:G6263-MONOMER.
ECOL316407:JW0476-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A9G4.
PROiP0A9G4.

Family and domain databases

InterProiIPR011789. CueR.
IPR009061. DNA-bd_dom_put.
IPR000551. MerR-type_HTH_dom.
[Graphical view]
PfamiPF13411. MerR_1. 1 hit.
[Graphical view]
PRINTSiPR00040. HTHMERR.
SMARTiSM00422. HTH_MERR. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 1 hit.
TIGRFAMsiTIGR02044. CueR. 1 hit.
PROSITEiPS00552. HTH_MERR_1. 1 hit.
PS50937. HTH_MERR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CueR (YbbI) of Escherichia coli is a MerR family regulator controlling expression of the copper exporter CopA."
    Stoyanov J.V., Hobman J.L., Brown N.L.
    Mol. Microbiol. 39:502-512(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  2. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / DH5-alpha.
  6. "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] [Europe PMC] [Abstract]
    Cited for: ROLE IN COPPER HOMEOSTASIS.
    Strain: K12.
  7. "An atypical linear Cu(I)-S2 center constitutes the high-affinity metal-sensing site in the CueR metalloregulatory protein."
    Chen K., Yuldasheva S., Penner-Hahn J.E., O'Halloran T.V.
    J. Am. Chem. Soc. 125:12088-12089(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE METAL-BINDING CENTER, MUTAGENESIS OF CYS-112; CYS-120; CYS-129 AND CYS-130.
  8. "The Escherichia coli copper-responsive copA promoter is activated by gold."
    Stoyanov J.V., Brown N.L.
    J. Biol. Chem. 278:1407-1410(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, MUTAGENESIS OF CYS-112; CYS-120; CYS-129 AND CYS-130.
  9. "Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR."
    Changela A., Chen K., Xue Y., Holschen J., Outten C.E., O'Halloran T.V., Mondragon A.
    Science 301:1383-1387(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS).

Entry informationi

Entry nameiCUER_ECOLI
AccessioniPrimary (citable) accession number: P0A9G4
Secondary accession number(s): P77565, Q2MBU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: March 16, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

CueR tightly binds Cu1+ via a linear S-Cu-S center.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.