Clp protease, ATP-binding subunit ClpX (IPR004487)

Short name: Clp_protease_ATP-bd_su_ClpX

Overlapping homologous superfamilies

Family relationships



ClpX is a member of the HSP (heat-shock protein) 100 family. Gel filtration and electron microscopy showed that ClpX subunits associate to form a six-membered ring that is stabilised by binding of ATP or nonhydrolysable analogs of ATP [PMID: 9575205]. It functions as an ATP-depedent [PMID: 9575205] molecular chaperone and is the regulatory subunit of the ClpXP protease [PMID: 12925799].

ClpXP is involved in DNA damage repair, stationary-phase gene expression, and ssrA-mediated protein quality control. To date more than 50 proteins include transcription factors, metabolic enzymes, and proteins involved in the starvation and oxidative stress responses have been identified as substrates [PMID: 12667450].

The N-terminal domain of ClpX is a C4-type zinc binding domain (ZBD) involved in substrate recognition. ZBD forms a very stable dimer that is essential for promoting the degradation of some typical ClpXP substrates such as lO and MuA [PMID: 12937164].

GO terms

Biological Process

GO:0006457 protein folding

Molecular Function

GO:0005524 ATP binding
GO:0051082 unfolded protein binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.