IPR003769
Adaptor protein ClpS, core
InterPro entry
Short name | ClpS_core |
Overlapping homologous superfamilies |
Description
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
[1].
ClpS is a small alpha/beta protein that consists of three α-helices connected to three antiparallel β-strands
[2]. 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.
References
1.ClpS, a substrate modulator of the ClpAP machine. Dougan DA, Reid BG, Horwich AL, Bukau B. Mol. Cell 9, 673-83, (2002). View articlePMID: 11931773
2.Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA. Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA. Nat. Struct. Biol. 9, 906-11, (2002). View articlePMID: 12426582
GO terms
biological process
molecular function
- None
cellular component
- None
Cross References
ENZYME
Genome Properties
Contributing Member Database Entry
- Pfam:PF02617
Representative structure
3o1f: P1 crystal form of E. coli ClpS at 1.4 A resolution