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clpP [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945082, updated on 11-Sep-2024

Summary

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Official Symbol
clpP
Primary source
ECOCYC:EG10158
Locus tag
b0437
See related
ASAP:ABE-0001515
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0431; lopP
Summary
ClpP can simultaneously bind ClpX and ClpA to form a heteromeric complex. [More information is available at EcoGene: EG10158]. ClpP is a serine protease with a chymotrypsin-like activity that is a part of the ClpAP, ClpAPX and ClpXP protease complexes . [More information is available at EcoCyc: EG10158].
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Genomic context

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Sequence:
NC_000913.3 (456677..457300)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene DNA-binding transcriptional dual regulator BolA Neighboring gene trigger factor Neighboring gene ATP-dependent Clp protease ATP-binding subunit ClpX Neighboring gene Lon protease

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. The activated ClpP peptidase forcefully grips a protein substrate. Walker SD, et al. Biophys J, 2022 Oct 18. PMID 36045571, Free PMC Article
  2. ClpXP protease targets long-lived DNA translocation states of a helicase-like motor to cause restriction alleviation. Simons M, et al. Nucleic Acids Res, 2014 Oct 29. PMID 25260590, Free PMC Article
  3. Structural determinants stabilizing the axial channel of ClpP for substrate translocation. Alexopoulos J, et al. Mol Microbiol, 2013 Oct. PMID 23927726
  4. ClpP: a structurally dynamic protease regulated by AAA+ proteins. Alexopoulos JA, et al. J Struct Biol, 2012 Aug. PMID 22595189
  5. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations. Kimber MS, et al. Structure, 2010 Jul 14. PMID 20637416

See all (202) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Structure of phosphorylated-like RssB, the adaptor delivering sigma[s] to the ClpXP proteolytic machinery, reveals an interface switch for activation.
    Title: Structure of phosphorylated-like RssB, the adaptor delivering σ(s) to the ClpXP proteolytic machinery, reveals an interface switch for activation.
  2. AAA+ protease-adaptor structures reveal altered conformations and ring specialization.
    Title: AAA+ protease-adaptor structures reveal altered conformations and ring specialization.
  3. The activated ClpP peptidase forcefully grips a protein substrate.
    Title: The activated ClpP peptidase forcefully grips a protein substrate.
  4. Division of labor between the pore-1 loops of the D1 and D2 AAA+ rings coordinates substrate selectivity of the ClpAP protease.
    Title: Division of labor between the pore-1 loops of the D1 and D2 AAA+ rings coordinates substrate selectivity of the ClpAP protease.
  5. Degradation of MinD oscillator complexes by Escherichia coli ClpXP.
    Title: Degradation of MinD oscillator complexes by Escherichia coli ClpXP.
  6. A split protease-E. coli ClpXP system quantifies protein-protein interactions in Escherichia coli cells.
    Title: A split protease-E. coli ClpXP system quantifies protein-protein interactions in Escherichia coli cells.
  7. ClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP.
    Title: ClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP.
  8. Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.
    Title: Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.
  9. ClpAP is a universal activator of the parDE system and that ParD is a universal substrate for ClpAP.
    Title: ClpAP protease is a universal factor that activates the parDE toxin-antitoxin system from a broad host range RK2 plasmid.
  10. Antirestriction activity of the mercury resistance nonconjugative transposon Tn5053 is controlled by the protease ClpXP
    Title: [Antirestriction activity of the mercury resistance nonconjugative transposon Tn5053 is controlled by the protease ClpXP].
Submit: New GeneRIF Correction See all GeneRIFs (29)

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP-dependent peptidase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ATP-dependent peptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP-dependent peptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables ATPase binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ATPase binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables serine-type endopeptidase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables serine-type endopeptidase activity IEA
Inferred from Electronic Annotation
more info
  
enables serine-type peptidase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables serine-type peptidase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in positive regulation of programmed cell death IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in proteasomal protein catabolic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein quality control for misfolded or incompletely synthesized proteins IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within protein quality control for misfolded or incompletely synthesized proteins IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in protein quality control for misfolded or incompletely synthesized proteins NAS
Non-traceable Author Statement
more info
 PubMed 
involved_in proteolysis IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within response to heat IEP
Inferred from Expression Pattern
more info
 PubMed 
acts_upstream_of_or_within response to radiation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within response to temperature stimulus EXP
Inferred from Experiment
more info
 PubMed 
Component Evidence Code Pubs
part_of HslUV protease complex IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol HDA PubMed 
part_of endopeptidase Clp complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of endopeptidase Clp complex IPI
Inferred from Physical Interaction
more info
 PubMed 
located_in membrane HDA PubMed 

General protein information

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Preferred Names
ATP-dependent Clp protease proteolytic subunit
NP_414971.1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    456677..457300
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_414971.1 ATP-dependent Clp protease proteolytic subunit [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_414971.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A418GLP1
    Conserved Domains (1) summary
    PRK00277
    Location:12 → 207
    clpP; ATP-dependent Clp protease proteolytic subunit; Reviewed
Nucleotide Protein
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