ATP-dependent Clp protease adaptor protein ClpS

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PDB 1r6q EBI.jpg
clpns with fragments
Symbol ClpS
Pfam PF02617
InterPro IPR003769
SCOP 1mbx

ClpS is an N-recognin in the N-end rule pathway. ClpS interacts with protein substrates that have a bulky hydrophobic residue (leucine, phenylalanine, tyrosine, and tryptophan) at the N-terminus. The protein substrate is then degraded by the ClpAP protease. [1]

In molecular biology, the ATP-dependent Clp protease adaptor protein ClpS is a bacterial protein. 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.[2]

ClpS is a small alpha/beta protein that consists of three alpha-helices connected to three antiparallel beta-strands.[3] 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.


  1. ^ Tasaki T, Sriram SM, Park KS, Kwon YT (10 April 2012). "The N-end rule pathway.". Annu Rev Biochem 81: 261–289. doi:10.1146/annurev-biochem-051710-093308. PMC 3610525. PMID 22524314. 
  2. ^ Dougan DA, Reid BG, Horwich AL, Bukau B (March 2002). "ClpS, a substrate modulator of the ClpAP machine". Mol. Cell 9 (3): 673–83. doi:10.1016/S1097-2765(02)00485-9. PMID 11931773. 
  3. ^ Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA (December 2002). "Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA". Nat. Struct. Biol. 9 (12): 906–11. doi:10.1038/nsb869. PMID 12426582. 

This article incorporates text from the public domain Pfam and InterPro IPR003769