D
IPR003769

Adaptor protein ClpS, core

InterPro entry
Short nameClpS_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

molecular function

  • None

cellular component

  • None

Cross References

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