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Protein

Transcriptional regulatory protein CpxR

Gene

cpxR

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

Functioni

Response regulator member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA (PubMed:7883164, PubMed:9401031). Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation (PubMed:11830644). Induced upon cell surface binding, subsequently induces genes it controls (cpxP, dsbA and spy, degP is only partially induced) (PubMed:11830644). Binds and activates transcription from the degP promoter (PubMed:7883164); binding is enhanced by phosphorylation (PubMed:9401031). This system combats a variety of extracytoplasmic protein-mediated toxicities by increasing the transcription of the periplasmic protease, DegP in concert with sigma factor E (PubMed:7883164), as well as that of CpxP protein. Other downstream effectors may include SrkA (PubMed:23416055).4 Publications

Enzyme regulationi

The two-component system is activated by envelope stress such as overexpression of some (misfolded) periplasmic proteins (PubMed:7883164, PubMed:9351822). Activated by spheroplasting (which removes the periplasm) in an autoregulatory cpxA-cpxR-dependent fashion (PubMed:10972835). Cpx two-component system is activated at pH 8.0; in a degP deletion mutant activation is halved (PubMed:9473036, PubMed:16166523). The CpxA kinase activity is inhibited by periplasmic accessory protein CpxP; proteolysis of CpxP relieves inhibition (PubMed:16166523, PubMed:17259177, PubMed:25207645).5 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi131 – 230OmpR/PhoB-typePROSITE-ProRule annotationAdd BLAST100

GO - Molecular functioni

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • negative regulation of transcription, DNA-templated Source: EcoCyc
  • phosphorelay signal transduction system Source: UniProtKB-KW
  • positive regulation of transcription, DNA-templated Source: CACAO
  • regulation of cell-substrate adhesion Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell adhesion, Stress response, Transcription, Transcription regulation, Two-component regulatory system

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:CPXR-MONOMER.
ECOL316407:JW3883-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional regulatory protein CpxR
Gene namesi
Name:cpxR
Synonyms:yiiA
Ordered Locus Names:b3912, JW3883
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10020. cpxR.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Loss of the Cpx envelope stress response (PubMed:10972835). A double cpxR-cpxA mutant decreases transcription of degP (PubMed:7883164). Cells are less sensitive to killing by nalidixic acid; double cpxR-srkA disruption mutants are as sensitive to killing as single srkA mutants, suggesting the SrkA protein kinase is partially regulated by CpxR. Hypersensitive to alkaline pH (greater than pH 8.8) (PubMed:9473036). Decreased numbers of stationary phase cells bind to hydrophobic surfaces, cellular adhesion has altered dynamic properties; no induction of cpxR when cells bind to hydrophobic surfaces (PubMed:11830644).5 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000810781 – 232Transcriptional regulatory protein CpxRAdd BLAST232

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei514-aspartylphosphatePROSITE-ProRule annotation1

Post-translational modificationi

Phosphorylated by CpxA.1 Publication2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP0AE88.
PaxDbiP0AE88.
PRIDEiP0AE88.

Expressioni

Inductioni

Induced about 3-fold when stationary phase cells bind to hydrophobic surfaces; requires direct contact with hydrophobic surfaces for up-regulation of Cpx activity (PubMed:11830644).1 Publication

Interactioni

Subunit structurei

Interacts with cognate sensor kinase CpxA.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
lysAP008612EBI-550918,EBI-553837

Protein-protein interaction databases

BioGridi4262645. 289 interactors.
DIPiDIP-47991N.
IntActiP0AE88. 11 interactors.
MINTiMINT-1292432.
STRINGi511145.b3912.

Structurei

Secondary structure

1232
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 7Combined sources5
Helixi11 – 23Combined sources13
Beta strandi27 – 33Combined sources7
Helixi34 – 40Combined sources7
Beta strandi47 – 50Combined sources4
Beta strandi55 – 57Combined sources3
Helixi59 – 66Combined sources8
Turni67 – 69Combined sources3
Beta strandi74 – 79Combined sources6
Helixi83 – 91Combined sources9
Beta strandi95 – 101Combined sources7
Helixi104 – 123Combined sources20
Beta strandi134 – 136Combined sources3
Beta strandi139 – 142Combined sources4
Turni143 – 146Combined sources4
Beta strandi147 – 150Combined sources4
Helixi159 – 170Combined sources12
Turni171 – 173Combined sources3
Helixi178 – 186Combined sources9
Helixi196 – 207Combined sources12
Beta strandi217 – 221Combined sources5
Turni222 – 224Combined sources3
Beta strandi225 – 228Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UHJX-ray1.90A/B/C1-123[»]
4UHKX-ray2.60A/B/C1-123[»]
4UHSX-ray5.00A/B/C1-123[»]
4UHTX-ray1.15A/B131-231[»]
ProteinModelPortaliP0AE88.
SMRiP0AE88.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 115Response regulatoryPROSITE-ProRule annotationAdd BLAST113

Sequence similaritiesi

Contains 1 OmpR/PhoB-type DNA-binding domain.PROSITE-ProRule annotation
Contains 1 response regulatory domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105E3W. Bacteria.
COG0745. LUCA.
HOGENOMiHOG000034819.
InParanoidiP0AE88.
KOiK07662.
OMAiSMIGYNV.
PhylomeDBiP0AE88.

Family and domain databases

CDDicd00383. trans_reg_C. 1 hit.
Gene3Di1.10.10.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR001867. OmpR/PhoB-type_DNA-bd.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00072. Response_reg. 1 hit.
PF00486. Trans_reg_C. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
SM00862. Trans_reg_C. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
PROSITEiPS51755. OMPR_PHOB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AE88-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKILLVDDD RELTSLLKEL LEMEGFNVIV AHDGEQALDL LDDSIDLLLL
60 70 80 90 100
DVMMPKKNGI DTLKALRQTH QTPVIMLTAR GSELDRVLGL ELGADDYLPK
110 120 130 140 150
PFNDRELVAR IRAILRRSHW SEQQQNNDNG SPTLEVDALV LNPGRQEASF
160 170 180 190 200
DGQTLELTGT EFTLLYLLAQ HLGQVVSREH LSQEVLGKRL TPFDRAIDMH
210 220 230
ISNLRRKLPD RKDGHPWFKT LRGRGYLMVS AS
Length:232
Mass (Da):26,312
Last modified:December 6, 2005 - v1
Checksum:i667FC2B246082F46
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14579 Unassigned DNA. Translation: AAC36868.1.
L19201 Genomic DNA. Translation: AAB03045.1.
U00096 Genomic DNA. Translation: AAC76894.1.
AP009048 Genomic DNA. Translation: BAE77397.1.
X13307 Genomic DNA. Translation: CAA31686.1.
M36795 Genomic DNA. Translation: AAA23599.1.
PIRiC65197.
RefSeqiNP_418348.1. NC_000913.3.
WP_001033722.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76894; AAC76894; b3912.
BAE77397; BAE77397; BAE77397.
GeneIDi948404.
KEGGiecj:JW3883.
eco:b3912.
PATRICi32123337. VBIEscCol129921_4029.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14579 Unassigned DNA. Translation: AAC36868.1.
L19201 Genomic DNA. Translation: AAB03045.1.
U00096 Genomic DNA. Translation: AAC76894.1.
AP009048 Genomic DNA. Translation: BAE77397.1.
X13307 Genomic DNA. Translation: CAA31686.1.
M36795 Genomic DNA. Translation: AAA23599.1.
PIRiC65197.
RefSeqiNP_418348.1. NC_000913.3.
WP_001033722.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UHJX-ray1.90A/B/C1-123[»]
4UHKX-ray2.60A/B/C1-123[»]
4UHSX-ray5.00A/B/C1-123[»]
4UHTX-ray1.15A/B131-231[»]
ProteinModelPortaliP0AE88.
SMRiP0AE88.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262645. 289 interactors.
DIPiDIP-47991N.
IntActiP0AE88. 11 interactors.
MINTiMINT-1292432.
STRINGi511145.b3912.

Proteomic databases

EPDiP0AE88.
PaxDbiP0AE88.
PRIDEiP0AE88.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76894; AAC76894; b3912.
BAE77397; BAE77397; BAE77397.
GeneIDi948404.
KEGGiecj:JW3883.
eco:b3912.
PATRICi32123337. VBIEscCol129921_4029.

Organism-specific databases

EchoBASEiEB0019.
EcoGeneiEG10020. cpxR.

Phylogenomic databases

eggNOGiENOG4105E3W. Bacteria.
COG0745. LUCA.
HOGENOMiHOG000034819.
InParanoidiP0AE88.
KOiK07662.
OMAiSMIGYNV.
PhylomeDBiP0AE88.

Enzyme and pathway databases

BioCyciEcoCyc:CPXR-MONOMER.
ECOL316407:JW3883-MONOMER.

Miscellaneous databases

PROiP0AE88.

Family and domain databases

CDDicd00383. trans_reg_C. 1 hit.
Gene3Di1.10.10.10. 1 hit.
InterProiIPR011006. CheY-like_superfamily.
IPR001867. OmpR/PhoB-type_DNA-bd.
IPR001789. Sig_transdc_resp-reg_receiver.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00072. Response_reg. 1 hit.
PF00486. Trans_reg_C. 1 hit.
[Graphical view]
SMARTiSM00448. REC. 1 hit.
SM00862. Trans_reg_C. 1 hit.
[Graphical view]
SUPFAMiSSF52172. SSF52172. 1 hit.
PROSITEiPS51755. OMPR_PHOB. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCPXR_ECOLI
AccessioniPrimary (citable) accession number: P0AE88
Secondary accession number(s): P16244, P76777, Q2M8K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: November 2, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.