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

Summary

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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: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; 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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Genomic context

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Sequence:: NC_000913.3 (457426..458700)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

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Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
Degradation of MinD oscillator complexes by Escherichia coli ClpXP.
Title: Degradation of MinD oscillator complexes by Escherichia coli ClpXP.
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.
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.
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.
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].
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.
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.
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.
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.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

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 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 denaturation	IDA Inferred from Direct Assay more info	PubMed
involved_in protein folding	IEA Inferred from Electronic Annotation more info
involved_in protein unfolding	IDA Inferred from Direct Assay more info	PubMed
involved_in proteolysis involved in protein catabolic process	IBA Inferred from Biological aspect of Ancestor more info

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
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 ClpX

NP_414972.1

EC 3.4.21.92

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

NC_000913.3 Reference assembly

Range

457426..458700

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_414972.1 ATP-dependent Clp protease ATP-binding subunit ClpX [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_414972.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A8S7S3P0, W1WWE4

Conserved Domains (1) summary

PRK05342
Location:4 → 417

clpX; ATP-dependent Clp protease ATP-binding subunit ClpX