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    clpA ATP-dependent Clp protease ATP-binding subunit ClpA [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945764, updated on 3-Dec-2024

    Summary

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    Official Symbol
    clpA
    Official Full Name
    ATP-dependent Clp protease ATP-binding subunit ClpA
    Primary source
    ECOCYC:EG10156
    Locus tag
    b0882
    See related
    ASAP:ABE-0003001
    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
    ECK0873; lopD
    Summary
    ClpA is an ATP-dependent molecular chaperone that serves as a substrate-specifying adapter for the ClpP serine protease in the ClpAP and ClpAXP protease complexes. [More information is available at EcoCyc: EG10156].
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    Genomic context

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    Sequence:
    NC_000913.3 (923264..925540)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene protein YljB Neighboring gene specificity factor for ClpA-ClpP chaperone-protease complex Neighboring gene tRNA-Ser Neighboring gene translation initiation factor IF-1

    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. ATPγS competes with ATP for binding at Domain 1 but not Domain 2 during ClpA catalyzed polypeptide translocation. Miller JM, et al. Biophys Chem, 2014 Jan. PMID 24362308, Free PMC Article
    2. Both ATPase domains of ClpA are critical for processing of stable protein structures. Kress W, et al. J Biol Chem, 2009 Nov 6. PMID 19726681, Free PMC Article
    3. Substrate recognition by the ClpA chaperone component of ClpAP protease. Hoskins JR, et al. J Biol Chem, 2000 Nov 10. PMID 10952988
    4. A role for the Clp protease in activating Mu-mediated DNA rearrangements. Shapiro JA. J Bacteriol, 1993 May. PMID 8386721, Free PMC Article
    5. The Escherichia coli ClpA molecular chaperone self-assembles into tetramers. Veronese PK, et al. Biochemistry, 2009 Oct 6. PMID 19650643

    See all (101) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. AAA+ protease-adaptor structures reveal altered conformations and ring specialization.
      Title: AAA+ protease-adaptor structures reveal altered conformations and ring specialization.
    2. 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.
    3. 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.
    4. 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.
    5. 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.
    6. These results demonstrate that ClpP allosterically impacts the polypeptide translocation activity of ClpA by reducing the cooperativity between ATP binding sites.
      Title: E. coli ClpA catalyzed polypeptide translocation is allosterically controlled by the protease ClpP.
    7. These results suggest that the presence of gamma phosphate may serve to switch ClpA into a conformational state with high peptide binding activity, whereas affinity is severely attenuated when ADP is bound.
      Title: Activity of E. coli ClpA bound by nucleoside diphosphates and triphosphates.
    8. Molecular mechanism of polypeptide translocation catalyzed by the Escherichia coli ClpA protein translocase
      Title: Molecular mechanism of polypeptide translocation catalyzed by the Escherichia coli ClpA protein translocase.
    9. one ClpS monomer is sufficient to direct the activity of the ClpA hexamer
      Title: A single ClpS monomer is sufficient to direct the activity of the ClpA hexamer.
    10. ATP hydrolysis in both domains of ClpA was required for efficiently processing substrates of high local stability.
      Title: Both ATPase domains of ClpA are critical for processing of stable protein structures.
    Submit: New GeneRIF Correction See all GeneRIFs (23)

    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 binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables ATP hydrolysis activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ATP hydrolysis activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP hydrolysis activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP-dependent peptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in cellular response to heat IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein quality control for misfolded or incompletely synthesized proteins NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    involved_in protein unfolding IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within protein unfolding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within proteolysis EXP
    Inferred from Experiment
    more info
    		 PubMed 
    acts_upstream_of_or_within response to oxidative stress IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of endopeptidase Clp complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    ATP-dependent Clp protease ATP-binding subunit ClpA
    NP_415403.1

    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
      923264..925540
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415403.1 ATP-dependent Clp protease ATP-binding subunit ClpA [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415403.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376FQ11, A0A376JYC5, A0A3L5H7G7, A0A776QUX1
      Conserved Domains (1) summary
      PRK11034
      Location:1 → 758
      clpA; ATP-dependent Clp protease ATP-binding subunit; Provisional
    Nucleotide Protein
    Heading Accession and Version

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