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

Gene ID: 945083, updated on 4-Feb-2026
Official Symbol
clpX
Official Full Name
ATP-dependent Clp protease ATP-binding subunit ClpX
Primary source
ECOCYC:EG10159
Locus tag
b0438
See related
ASAP:ABE-0001517
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0432; lopC
Summary
ClpX is an ATP-dependent molecular chaperone that serves as a substrate-specifying adapter for the ClpP serine protease in the ClpXP and ClpAXP protease complexes. [More information is available at EcoCyc: EG10159].
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Sequence:
NC_000913.3 (457426..458700)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene trigger factor Neighboring gene ATP-dependent Clp protease proteolytic subunit Neighboring gene Lon protease Neighboring gene DNA-binding protein HU-beta

Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. Wawrzynow A, et al. EMBO J, 1995 May 1. PMID 7743994, Free PMC Article
  2. The replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperone. Konieczny I, et al. Proc Natl Acad Sci U S A, 1997 Dec 23. PMID 9405620, Free PMC Article
  3. How to pick a protein and pull at it. Inobe T, et al. Nat Struct Mol Biol, 2008 Nov. PMID 18985068
  4. ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway. Levchenko I, et al. Genes Dev, 1997 Jun 15. PMID 9203582
  5. Specificity in substrate and cofactor recognition by the N-terminal domain of the chaperone ClpX. Thibault G, et al. Proc Natl Acad Sci U S A, 2006 Nov 21. PMID 17090685, Free PMC Article

See all (142) 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. Degradation of MinD oscillator complexes by Escherichia coli ClpXP.
    Title: Degradation of MinD oscillator complexes by Escherichia coli ClpXP.
  3. 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.
  4. Results indicate that hinge-linker length and flexibility are optimized for efficient substrate unfolding and support a model in which the hinge-linker elements of ClpX facilitate efficient degradation both by maintaining proper ring geometry and facilitating subunit-subunit communication.
    Title: Hinge-Linker Elements in the AAA+ Protein Unfoldase ClpX Mediate Intersubunit Communication, Assembly, and Mechanical Activity.
  5. When the weak C-tag signal is replaced with a The AAA + unfoldase ClpX specifically recognizes two classes of recognition tags in the MuA transposase,specific features of these MuA tag classes direct ClpX to the biologically important reaction path.
    Title: Deciphering the Roles of Multicomponent Recognition Signals by the AAA+ Unfoldase ClpX.
  6. 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].
  7. When ClpX encounters a folded protein, it either overcomes this mechanical barrier or slips on the polypeptide before making another unfolding attempt. Binding of ClpP decreases the slip probability and enhances the unfolding efficiency of ClpX.
    Title: ClpX(P) generates mechanical force to unfold and translocate its protein substrates.
  8. Together, our results suggested that ClpXP modulates cell division through degradation of FtsZ and possibly other cell division components that function downstream of FtsZ ring assembly.
    Title: The interplay of ClpXP with the cell division machinery in Escherichia coli.
  9. results also reveal highly conserved residues in the ClpX-binding peptides of both E. coli SspB and C. crescentus SspBalpha that play no detectable role in ClpX-binding or substrate delivery.
    Title: Versatile modes of peptide recognition by the ClpX N domain mediate alternative adaptor-binding specificities in different bacterial species.
  10. The crystal structures presented here reveal striking asymmetry in ring hexamers of nucleotide-free and nucleotide-bound ClpX.
    Title: Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.
Submit: New GeneRIF Correction See all GeneRIFs (26)
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ATP binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
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 ATP-dependent protein folding chaperone IEA
Inferred from Electronic Annotation
more info
  
enables disordered domain specific binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables protease binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables protein dimerization activity IEA
Inferred from Electronic Annotation
more info
  
enables unfolded protein binding IEA
Inferred from Electronic Annotation
more info
  
enables zinc ion binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in cell division IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in cell division IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in protein catabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein folding IEA
Inferred from Electronic Annotation
more info
  
involved_in protein unfolding IDA
Inferred from Direct Assay
more info
 PubMed 
Component Evidence Code Pubs
part_of HslUV protease complex IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of HslUV protease complex IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
Preferred Names
ATP-dependent Clp protease ATP-binding subunit ClpX
NP_414972.1

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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
    457426..458700
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_414972.1 ATP-dependent Clp protease ATP-binding subunit ClpX

    See identical proteins and their annotated locations for NP_414972.1

    Status: REVIEWED

    UniProtKB/TrEMBL
    A0A8S7S3P0, W1WWE4
    Conserved Domains (1) summary
    PRK05342
    Location:4 → 417
    clpX; ATP-dependent Clp protease ATP-binding subunit ClpX
Nucleotide Protein
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