<p>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 [<cite idref="PUB00020759"/>]. 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 [<cite idref="PUB00020750"/>, <cite idref="PUB00020760"/>]. A small adaptor-like protein, ClpS, modulates the activity of ClpA and is an important regulatory factor for this protein [<cite idref="PUB00020738"/>]. It protects ClpA from autodegradation and appears to redirect its activity away from soluble proteins and toward aggregated proteins.</p><p>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 [<cite idref="PUB00028807"/>].</p>