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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. Site-directed mutagenesis of the Cys residues in ClpA, the ATPase component of protease Ti (ClpAP) in Escherichia coli. Seol JH, et al. Biol Chem, 1997 Oct. PMID 9372193
  2. Synchrotron protein footprinting supports substrate translocation by ClpA via ATP-induced movements of the D2 loop. Bohon J, et al. Structure, 2008 Aug 6. PMID 18682217, Free PMC Article
  3. Mutational analysis demonstrates different functional roles for the two ATP-binding sites in ClpAP protease from Escherichia coli. Singh SK, et al. J Biol Chem, 1994 Nov 25. PMID 7961938
  4. 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
  5. Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding. Erbse AH, et al. FEBS J, 2008 Apr. PMID 18279386

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
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