The domain within your query sequence starts at position 222 and ends at position 301; the E-value for the ClpS domain shown below is 6.2e-26.
EKSDTYYCMLFNDEVHTYEQVIYTLQKAVNCTQKEAIGFATTVDRDGRRSVRYGDFQYCD QAKTVIVRNTSRQTKPLKVQ
ClpS |
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PFAM accession number: | PF02617 |
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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