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Protein

Periplasmic protein CpxP

Gene

cpxP

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

Functioni

Acts as an auxiliary protein in the Cpx two-component envelope stress response system, helping modulate the Cpx response systems response to some inducers (PubMed:25207645, PubMed:16303867). Binds the periplasmic domain of sensor histidine kinase CpxA, inhibiting induction of the Cpx envelope stress response in the absence of inducer; overexpression decreases Cpx pathway activity (PubMed:16166523, PubMed:21317318). Some periplasmic stimulii (shown for P pili subunit PapE and probably 0.3 M NaCl) increase CpxP's susceptibility to DegP, leading to CpxP degradation, inducing the Cpx pathway (PubMed:16166523, PubMed:16303867). Aids in combating extracytoplasmic protein-mediated toxicity (PubMed:9473036, PubMed:16303867, PubMed:21239493). Overexpression leads to degradation by DegP of misfolded P pili subunits in the periplasm (tested using PapE) (PubMed:21239493). Inhibits autophosphorylation of CpxA in reconstituted liposomes by 50% but has no effect on phosphatase activity of CpxA (PubMed:17259177, PubMed:21239493). Has mild protein chaperone activity (PubMed:21317898, PubMed:21239493).8 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • unfolded protein binding Source: EcoCyc

GO - Biological processi

  • negative regulation of transcription, DNA-templated Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciEcoCyc:G7816-MONOMER.
ECOL316407:JW5558-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic protein CpxP1 Publication
Alternative name(s):
ORF_o1671 Publication
Periplasmic accessory protein CpxP
Gene namesi
Name:cpxP1 Publication
Synonyms:yiiO
Ordered Locus Names:b4484, JW5558
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11872. cpxP.

Subcellular locationi

  • Periplasm 2 Publications

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

Hypersensitive to alkaline pH (greater than pH 8.8) (PubMed:9473036). Increased accumulation and toxicity of overexpressed, misfolded periplasmic proteins (PubMed:16303867).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi55 – 551Q → P: No longer inhibits Cpx pathway, protein more susceptible to DegP. 2 Publications
Mutagenesisi56 – 561R → Q: No longer interacts with CpxA. 1 Publication
Mutagenesisi59 – 591M → T: No longer inhibits Cpx pathway, protein more susceptible to DegP. 1 Publication
Mutagenesisi60 – 601R → Q: No longer inhibits Cpx pathway. 1 Publication
Mutagenesisi61 – 611D → E or V: No longer inhibits Cpx pathway. 1 Publication
Mutagenesisi103 – 1031A → D or G: Decreased protein stability, significantly reduced degradation of PapE. 1 Publication
Mutagenesisi107 – 1071I → D: Decreased protein stability, significantly reduced degradation of PapE. 1 Publication
Mutagenesisi107 – 1071I → G or N: Decreased protein stability, wild-type degradation of PapE. 1 Publication
Mutagenesisi108 – 1081A → D: Decreased protein stability, significantly reduced degradation of PapE. 1 Publication
Mutagenesisi108 – 1081A → G: Decreased protein stability, wild-type degradation of PapE. 1 Publication
Mutagenesisi108 – 1081A → V: Decreased protein stability, significantly reduced degradation of PapE, retains most Cpx inhibition activity. 2 Publications
Mutagenesisi128 – 1281Q → H: No longer inhibits Cpx pathway in wild-type cells, protein more susceptible to DegP, in the absence of DegP protease partially inhibits Cpx. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 166145Periplasmic protein CpxPPRO_0000020992Add
BLAST

Post-translational modificationi

Degraded by DegP; some CpxP mutant proteins are more susceptible to the protease than others (PubMed:16166523). Degradation probably occurs when CpxP is associated with some misfolded proteins; overexpression of PapE leads to DegP-mediated degradation of CpxP and PapE, which requires the N-terminus of PapE. Overexpression of NlpE does not induce this degradation however (PubMed:16303867).2 Publications

Proteomic databases

PaxDbiP0AE85.

Expressioni

Inductioni

Induced by envelope stress such as overexpression of misfolded periplasmic proteins (PubMed:9351822). Induced by alkaine pH (tested up to pH 8.4) (PubMed:9473036, PubMed:16166523). Induction is decreased in a degP deletion (PubMed:16166523). Transcription is stimulated by the Cpx two-component signal transduction pathway; sigma factor E (rpoE) is not involved (PubMed:9351822, PubMed:9473036, PubMed:10972835). Transcription induced by spheroplasting, which removes the periplasm and thus this protein; if the protein is anchored to the outer surface of the inner membrane induction does not occur (PubMed:10972835). Induced in persister cells (PubMed:16768798).5 Publications

Interactioni

Subunit structurei

Homodimer; it might alter shape slightly at pH 8.0 when Cpx is induced (PubMed:21317318, PubMed:21239493). Binds the periplasmic sensor domain of CpxA (PubMed:16166523, PubMed:21317318, PubMed:21239493, PubMed:25207645). Interaction with CpxA is not seen in vivo when cells are grown in 0.3 M NaCl, or if the misfolded P pili protein PapE is overexpressed (PubMed:25207645).1 Publication3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-6413881,EBI-6413881

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • unfolded protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262646. 126 interactions.
DIPiDIP-47937N.
STRINGi511145.b4484.

Structurei

Secondary structure

1
166
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni45 – 484Combined sources
Helixi53 – 6917Combined sources
Helixi75 – 8511Combined sources
Beta strandi87 – 893Combined sources
Helixi92 – 12130Combined sources
Helixi126 – 14217Combined sources
Helixi146 – 1494Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ITFX-ray1.45A/B21-150[»]
3QZCX-ray2.85A/B40-151[»]
ProteinModelPortaliP0AE85.
SMRiP0AE85. Positions 40-151.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AE85.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 617Important for protein stability, probably interacts with CpxA1 Publication
Regioni151 – 16616Not required for activation of CpxA or to induce degradation of misfolded P pili subunits1 PublicationAdd
BLAST

Domaini

A region in the N-terminus (residues 55-61) probably interacts with the periplasmic sensor domain of CpxA to inhibit its kinase activity and is also important for CpxP stability (PubMed:16166523). The homodimer has an elongated cradle shape; a hydrophobic cleft on the convex face may interact with periplasmic protein PapE (PubMed:21239493).2 Publications

Sequence similaritiesi

Belongs to the CpxP/Spy family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105FMW. Bacteria.
COG3678. LUCA.
HOGENOMiHOG000285733.
InParanoidiP0AE85.
KOiK06006.
OMAiTTIDEMH.

Family and domain databases

CDDicd09916. CpxP_like. 1 hit.
InterProiIPR012899. LTXXQ.
[Graphical view]
PfamiPF07813. LTXXQ. 1 hit.
[Graphical view]
PIRSFiPIRSF034445. CpxP_Spy. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AE85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIVTAAVMA STLAVSSLSH AAEVGSGDNW HPGEELTQRS TQSHMFDGIS
60 70 80 90 100
LTEHQRQQMR DLMQQARHEQ PPVNVSELET MHRLVTAENF DENAVRAQAE
110 120 130 140 150
KMANEQIARQ VEMAKVRNQM YRLLTPEQQA VLNEKHQQRM EQLRDVTQWQ
160
KSSSLKLLSS SNSRSQ
Length:166
Mass (Da):18,965
Last modified:December 6, 2005 - v1
Checksum:iBD517D2D14D90209
GO

Sequence cautioni

The sequence AAB03046 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19201 Genomic DNA. Translation: AAB03046.1. Different initiation.
U00096 Genomic DNA. Translation: AAT48235.1.
AP009048 Genomic DNA. Translation: BAE77396.1.
RefSeqiWP_001223800.1. NZ_LN832404.1.
YP_026277.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48235; AAT48235; b4484.
BAE77396; BAE77396; BAE77396.
GeneIDi2847688.
KEGGiecj:JW5558.
eco:b4484.
PATRICi32123339. VBIEscCol129921_4030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19201 Genomic DNA. Translation: AAB03046.1. Different initiation.
U00096 Genomic DNA. Translation: AAT48235.1.
AP009048 Genomic DNA. Translation: BAE77396.1.
RefSeqiWP_001223800.1. NZ_LN832404.1.
YP_026277.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ITFX-ray1.45A/B21-150[»]
3QZCX-ray2.85A/B40-151[»]
ProteinModelPortaliP0AE85.
SMRiP0AE85. Positions 40-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262646. 126 interactions.
DIPiDIP-47937N.
STRINGi511145.b4484.

Proteomic databases

PaxDbiP0AE85.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48235; AAT48235; b4484.
BAE77396; BAE77396; BAE77396.
GeneIDi2847688.
KEGGiecj:JW5558.
eco:b4484.
PATRICi32123339. VBIEscCol129921_4030.

Organism-specific databases

EchoBASEiEB1818.
EcoGeneiEG11872. cpxP.

Phylogenomic databases

eggNOGiENOG4105FMW. Bacteria.
COG3678. LUCA.
HOGENOMiHOG000285733.
InParanoidiP0AE85.
KOiK06006.
OMAiTTIDEMH.

Enzyme and pathway databases

BioCyciEcoCyc:G7816-MONOMER.
ECOL316407:JW5558-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AE85.
PROiP0AE85.

Family and domain databases

CDDicd09916. CpxP_like. 1 hit.
InterProiIPR012899. LTXXQ.
[Graphical view]
PfamiPF07813. LTXXQ. 1 hit.
[Graphical view]
PIRSFiPIRSF034445. CpxP_Spy. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCPXP_ECOLI
AccessioniPrimary (citable) accession number: P0AE85
Secondary accession number(s): O65939, P32158, Q2M8L0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: September 7, 2016
This is version 79 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.