The domain within your query sequence starts at position 221 and ends at position 301; the E-value for the ClpS domain shown below is 8e-24.



PFAM accession number:PF02617
Interpro abstract (IPR003769):

In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. ClpS directly influences the ClpAP machine by binding to the N-terminal domain of the chaperone ClpA. The degradation of ClpAP substrates, both SsrA-tagged proteins and ClpA itself, is specifically inhibited by ClpS. ClpS modifies ClpA substrate specificity, potentially redirecting degradation by ClpAP toward aggregated proteins [ (PUBMED:11931773) ].

ClpS is a small alpha/beta protein that consists of three alpha-helices connected to three antiparallel beta-strands [ (PUBMED:12426582) ]. The protein has a globular shape, with a curved layer of three antiparallel alpha-helices over a twisted antiparallel beta-sheet. Dimerization of ClpS may occur through its N-terminal domain. This short extended N-terminal region in ClpS is followed by the central seven-residue beta-strand, which is flanked by two other beta-strands in a small beta-sheet.

GO process:protein catabolic process (GO:0030163)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ClpS