Description

IPR036628 is a Clp, N-terminal domain superfamily.

<p>ClpA is an ATP-dependent chaperone and part of the ClpAP protease that participates in regulatory protein degradation and the dissolution and degradation of protein aggregates [[cite:PUB00020759]]. ClpA recognises sequences in specific proteins, which it then unfolds in an ATP-dependent manner and transports into the degradation chamber of the associated ClpP protein [[cite:PUB00020750], [cite:PUB00020760]]. A small adaptor-like protein, ClpS, modulates the activity of ClpA and is an important regulatory factor for this protein [[cite:PUB00020738]]. It protects ClpA from autodegradation and appears to redirect its activity away from soluble proteins and toward aggregated proteins.</p> <p>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 [[cite:PUB00094776], [cite:PUB00030547], [cite:PUB00094777], [cite:PUB00048252], [cite:PUB00094775], [cite:PUB00094778]].</p> <p>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 [[cite:PUB00030547], [cite:PUB00094777], [cite:PUB00048252]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 35

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: