UniProt functional annotation for P63284



	UniProt functional annotation for P63284

UniProt code: P63284.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

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:10982797, ECO:0000269|PubMed:12624113, ECO:0000269|PubMed:14640692}.

Subunit: Homohexamer. The oligomerization is ATP-dependent. {ECO:0000269|PubMed:11061966}.

Subcellular location: Cytoplasm {ECO:0000269|PubMed:8376377}.

Induction: By heat shock and other environmental stresses.

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.

Miscellaneous: One peptide binds per ClpB hexamer; the binding site is formed only upon ATP-driven oligomerization.

Miscellaneous: [Isoform ClpB-3]: ClpB-3 ATPase activity is not activated by proteins, as it is in ClpB. {ECO:0000305}.

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

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



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:10982797, ECO:0000269\|PubMed:12624113, ECO:0000269\|PubMed:14640692}.


Subunit:		Homohexamer. The oligomerization is ATP-dependent. {ECO:0000269\|PubMed:11061966}.
Subcellular location:		Cytoplasm {ECO:0000269\|PubMed:8376377}.
Induction:		By heat shock and other environmental stresses.
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.
Miscellaneous:		One peptide binds per ClpB hexamer; the binding site is formed only upon ATP-driven oligomerization.
Miscellaneous:		[Isoform ClpB-3]: ClpB-3 ATPase activity is not activated by proteins, as it is in ClpB. {ECO:0000305}.
Similarity:		Belongs to the ClpA/ClpB family. {ECO:0000305}.