Homologous Superfamily

Clp, N-terminal domain superfamily (IPR036628)

Short name: Clp_N_dom_sf

Overlapping entries


ClpA is an ATP-dependent chaperone and part of the ClpAP protease that participates in regulatory protein degradation and the dissolution and degradation of protein aggregates [PMID: 2186030]. ClpA recognises sequences in specific proteins, which it then unfolds in an ATP-dependent manner and transports into the degradation chamber of the associated ClpP protein [PMID: 10485712, PMID: 11287666]. A small adaptor-like protein, ClpS, modulates the activity of ClpA and is an important regulatory factor for this protein [PMID: 12235156]. It protects ClpA from autodegradation and appears to redirect its activity away from soluble proteins and toward aggregated proteins.

This entry represents the double Clp-N motif domain found at the N terminus of ATP-dependent Clp proteases. This N-terminal domain interacts with the D1 domain found in Cpl proteases in a fashion similar to that seen in adaptor-binding domains of other AAA(+) proteins [PMID: 12205096].

GO terms

Biological Process

GO:0019538 protein metabolic process

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

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