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PROSITE documentation PDOC51903 [for PROSITE entry PS51903]

Clp repeat (R) domain profile





Description

Molecular chaperones recognize unfolded or misfolded proteins by binding to hydrophobic surface patches not normally exposed in the native proteins. Members of the Clp/Hsp100 family of chaperones are present in eubacteria and within organelles of all eukaryotes, promoting disaggregation and disassembly of protein complexes and participating in energy-dependent protein degradation. The ClpA, ClpB, and ClpC subfamilies of the Clp/Hsp100 ATPases contain a conserved N-terminal domain of ~150 amino acids, which in turn consists of two repeats of ~75 residues. Although the Clp repeat (R) domain contains two approximate sequence repeats, it behaves as a single cooperatively folded unit. The Clp R domain is thought to provide a means for regulating the specificity of and to enlarge the substrate pool available to Clp/Hsp100 chaperone or protease complexes. These roles can be assisted through the binding of an adaptor protein. Adaptor proteins bind to the Clp R domain, modulate the target specificity of the Clp/Hsp100 complex to a particular substrate of interest, and may also regulate the activity of the complex [1,2,3,4,5,6].

The Clp R domain is monomeric and partially α helical. It is a single folding unit with pseudo 2-fold symmetry. The Clp R domain structure consists of two four-helix bundles connected by a flexible loop [2,3,4].

The profile we developed covers the entire Clp R domain.

Last update:

August 2019 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

CLP_R, PS51903; Clp repeat (R) domain profile  (MATRIX)


References

1AuthorsLo J.H. Baker T.A. Sauer R.T.
TitleCharacterization of the N-terminal repeat domain of Escherichia coli ClpA-A class I Clp/HSP100 ATPase.
SourceProtein. Sci. 10:551-559(2001).
PubMed ID11344323
DOI10.1110/ps.41401

2AuthorsXia D. Esser L. Singh S.K. Guo F. Maurizi M.R.
TitleCrystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone.
SourceJ. Struct. Biol. 146:166-179(2004).
PubMed ID15037248
DOI10.1016/j.jsb.2003.11.025

3AuthorsWang P. Li J. Weaver C. Lucius A. Sha B.
TitleCrystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 in dissolving prions.
SourceActa Crystallogr. D. Struct. Biol. 73:365-372(2017).
PubMed ID28375147
DOI10.1107/S2059798317002662

4AuthorsKojetin D.J. McLaughlin P.D. Thompson R.J. Dubnau D. Prepiak P. Rance M. Cavanagh J.
TitleStructural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions.
SourceJ. Mol. Biol. 387:639-652(2009).
PubMed ID19361434
DOI10.1016/j.jmb.2009.01.046

5AuthorsKim J. Kimber M.S. Nishimura K. Friso G. Schultz L. Ponnala L. van Wijk K.J.
TitleStructures, Functions, and Interactions of ClpT1 and ClpT2 in the Clp Protease System of Arabidopsis Chloroplasts.
SourcePlant. Cell. 27:1477-1496(2015).
PubMed ID25921872
DOI10.1105/tpc.15.00106

6AuthorsLiang Y. Ward S. Li P. Bennett T. Leyser O.
TitleSMAX1-LIKE7 Signals from the Nucleus to Regulate Shoot Development in Arabidopsis via Partially EAR Motif-Independent Mechanisms.
SourcePlant. Cell. 28:1581-1601(2016).
PubMed ID27317673
DOI10.1105/tpc.16.00286



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