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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)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
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)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.

Protein-protein interaction databases

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

Structurei

Secondary structure

1135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 10Combined sources8
Helixi14 – 22Combined sources9
Helixi41 – 55Combined sources15
Helixi60 – 71Combined sources12
Turni73 – 76Combined sources4
Helixi77 – 110Combined sources34
Beta strandi115 – 118Combined sources4
Helixi121 – 126Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.

Sequence similaritiesi

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

Phylogenomic databases

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

Family and domain databases

CDDicd01108. HTH_CueR. 1 hit.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259848. 11 interactors.
DIPiDIP-51206N.
IntActiP0A9G4. 4 interactors.
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.
PhylomeDBiP0A9G4.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A9G4.
PROiP0A9G4.

Family and domain databases

CDDicd01108. HTH_CueR. 1 hit.
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...

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: November 2, 2016
This is version 99 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.