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Protein

HTH-type transcriptional regulator CueR

Gene

cueR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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.3 Publications

Miscellaneous

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi112Copper(1+)1
Metal bindingi120Copper(1+)1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi4 – 23H-T-H motifPROSITE-ProRule annotationAdd BLAST20

GO - Molecular functioni

GO - Biological processi

  • positive regulation of transcription, DNA-templated Source: EcoCyc
  • transcription, DNA-templated Source: EcoCyc

Keywordsi

Molecular functionActivator, DNA-binding
Biological processTranscription, Transcription regulation
LigandCopper, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:G6263-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
HTH-type transcriptional regulator CueR
Alternative name(s):
Copper efflux regulator
Copper export regulator
Gene namesi
Name:cueR1 Publication
Synonyms:copR1 Publication, ybbI
Ordered Locus Names:b0487, JW0476
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13256 cueR

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Loss of Cu-induction of copA, forms smaller than wild-type colonies when grown on 2 mM CuSO4 (PubMed:11167016).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi112C → S: Loss of sensitivity to copper. 2 Publications1
Mutagenesisi120C → S: Loss of sensitivity to copper. 2 Publications1
Mutagenesisi129C → S: No effect on response to copper. 2 Publications1
Mutagenesisi130C → S: No effect on response to copper. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000981111 – 135HTH-type transcriptional regulator CueRAdd BLAST135

Proteomic databases

PaxDbiP0A9G4
PRIDEiP0A9G4

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1117686,EBI-1117686

GO - Molecular functioni

Protein-protein interaction databases

BioGridi4259848, 11 interactors
DIPiDIP-51206N
IntActiP0A9G4, 4 interactors
STRINGi316385.ECDH10B_0444

Structurei

Secondary structure

1135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP0A9G4
SMRiP0A9G4
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A9G4

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 69HTH merR-typePROSITE-ProRule annotationAdd BLAST69

Domaini

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

Phylogenomic databases

eggNOGiENOG4108Z6Z Bacteria
COG0789 LUCA
HOGENOMiHOG000266076
InParanoidiP0A9G4
KOiK19591
OMAiYDERAVH
PhylomeDBiP0A9G4

Family and domain databases

CDDicd01108 HTH_CueR, 1 hit
InterProiView protein in InterPro
IPR011789 CueR
IPR009061 DNA-bd_dom_put_sf
IPR000551 MerR-type_HTH_dom
PfamiView protein in Pfam
PF13411 MerR_1, 1 hit
PRINTSiPR00040 HTHMERR
SMARTiView protein in SMART
SM00422 HTH_MERR, 1 hit
SUPFAMiSSF46955 SSF46955, 1 hit
TIGRFAMsiTIGR02044 CueR, 1 hit
PROSITEiView protein in PROSITE
PS00552 HTH_MERR_1, 1 hit
PS50937 HTH_MERR_2, 1 hit

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
PATRICifig|1411691.4.peg.1789

Similar proteinsi

Entry informationi

Entry nameiCUER_ECOLI
AccessioniPrimary (citable) accession number: P0A9G4
Secondary accession number(s): P77565, Q2MBU0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: March 28, 2018
This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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