Chaperone protein htpG; Molecular chaperone. Has ATPase activity.

Co-chaperone HSP-70 protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of [...]

ClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family.

60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.

Chaperone ClpB; 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; Belongs to the ClpA/ClpB family.

ClpB is a homohexamer that is a part of a stress-induced multi-chaperone system involved in the recovery of the cell from heat-induced damage, in cooperation with dnaK, dnaJ and grpE. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates contributing to the solubilization and refolding of denatured protein aggregates by dnaK; Contains 2 AAA ATPase domains; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family.

Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...]

Peptidyl-prolyl cis-trans isomerase, or PPIase or rotamase, accelerates the folding of proteins. It catalyzes the peptidyl-prolyl isomerisation during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilised in the cis conformation in oligopeptides; Contains a N-terminal Cyclophilin type PPIase/CLD and a C-terminal FKBP-type peptidyl-prolyl cis- trans isomerase; Localized in the cytoplasm; High confidence in function and specificity.

10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.