UniProt functional annotation for Q9RA63



	UniProt functional annotation for Q9RA63

UniProt code: Q9RA63.

Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).

Taxonomy: Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.

Function: Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. {ECO:0000269|PubMed:10377389}.

Subunit: Homohexamer. The oligomerization is ATP-dependent. {ECO:0000269|PubMed:11741950, ECO:0000269|PubMed:14567920}.

Subcellular location: Cytoplasm {ECO:0000305}.

Domain: The Clp repeat (R) domain probably functions as a substrate- discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer.

Similarity: Belongs to the ClpA/ClpB family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
Taxonomy:		Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.



Function:		Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. {ECO:0000269\|PubMed:10377389}.


Subunit:		Homohexamer. The oligomerization is ATP-dependent. {ECO:0000269\|PubMed:11741950, ECO:0000269\|PubMed:14567920}.
Subcellular location:		Cytoplasm {ECO:0000305}.
Domain:		The Clp repeat (R) domain probably functions as a substrate- discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer.
Similarity:		Belongs to the ClpA/ClpB family. {ECO:0000305}.