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

    Gene ID: 945082, updated on 3-Dec-2024

    Summary

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    Official Symbol
    clpP
    Official Full Name
    ATP-dependent Clp protease proteolytic subunit
    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. Turned on for degradation: ATPase-independent degradation by ClpP. Bewley MC, et al. J Struct Biol, 2009 Feb. PMID 19038348, Free PMC Article
    2. The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5. Kroh HE, et al. J Bacteriol, 1990 Oct. PMID 2211522, Free PMC Article
    3. Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli ClpP is a tetradecamer with an axial pore. Flanagan JM, et al. Biochemistry, 1995 Aug 29. PMID 7662672
    4. ClpP: a structurally dynamic protease regulated by AAA+ proteins. Alexopoulos JA, et al. J Struct Biol, 2012 Aug. PMID 22595189
    5. Quantitative NMR spectroscopy of supramolecular complexes: dynamic side pores in ClpP are important for product release. Sprangers R, et al. Proc Natl Acad Sci U S A, 2005 Nov 15. PMID 16263929, Free PMC Article

    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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    Homology

    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
    Heading Accession and Version

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