| Primary Identifier | IPR022935 | Type | Family |
| Short Name | ClpS |
| description | This entry includes ClpS from bacteria and chloroplastic CLPS1/2 from plants. ClpS binds directly to N-terminal destabilising residues through its substrate-binding site distal to the ClpS-ClpA interface, and targets these substrates to the ClpAP protease for degradation [, ].ClpS is a small alpha/beta protein that consists of three α-helices connected to three antiparallel β-strands []. The protein has a globular shape, with a curved layer of three antiparallel α-helices over a twisted antiparallel β-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 β-strand, which is flanked by two other β-strands in a small β-sheet. |
