Clp, N-terminal (IPR004176)

Short name: Clp_N

Overlapping homologous superfamilies

Domain relationships



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].

Contributing signatures

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