PROSITE documentation PDOC51903 [for PROSITE entry PS51903]Clp repeat (R) domain profile
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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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Lo J.H. Baker T.A. Sauer R.T. |
Title | Characterization of the N-terminal repeat domain of Escherichia coli ClpA-A class I Clp/HSP100 ATPase. | |
Source | Protein. Sci. 10:551-559(2001). | |
PubMed ID | 11344323 | |
DOI | 10.1110/ps.41401 |
2 | Authors | Xia D. Esser L. Singh S.K. Guo F. Maurizi M.R. |
Title | Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone. | |
Source | J. Struct. Biol. 146:166-179(2004). | |
PubMed ID | 15037248 | |
DOI | 10.1016/j.jsb.2003.11.025 |
3 | Authors | Wang P. Li J. Weaver C. Lucius A. Sha B. |
Title | Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 in dissolving prions. | |
Source | Acta Crystallogr. D. Struct. Biol. 73:365-372(2017). | |
PubMed ID | 28375147 | |
DOI | 10.1107/S2059798317002662 |
4 | Authors | Kojetin D.J. McLaughlin P.D. Thompson R.J. Dubnau D. Prepiak P. Rance M. Cavanagh J. |
Title | Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions. | |
Source | J. Mol. Biol. 387:639-652(2009). | |
PubMed ID | 19361434 | |
DOI | 10.1016/j.jmb.2009.01.046 |
5 | Authors | Kim J. Kimber M.S. Nishimura K. Friso G. Schultz L. Ponnala L. van Wijk K.J. |
Title | Structures, Functions, and Interactions of ClpT1 and ClpT2 in the Clp Protease System of Arabidopsis Chloroplasts. | |
Source | Plant. Cell. 27:1477-1496(2015). | |
PubMed ID | 25921872 | |
DOI | 10.1105/tpc.15.00106 |
6 | Authors | Liang Y. Ward S. Li P. Bennett T. Leyser O. |
Title | SMAX1-LIKE7 Signals from the Nucleus to Regulate Shoot Development in Arabidopsis via Partially EAR Motif-Independent Mechanisms. | |
Source | Plant. Cell. 28:1581-1601(2016). | |
PubMed ID | 27317673 | |
DOI | 10.1105/tpc.16.00286 |
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