Uncharacterized protein; Belongs to the GroES chaperonin family.

Endoplasmic reticulum chaperone BiP homolog; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Required for ER dynamics during the first embryonic cell divisions. Specifically, controls ER transition into sheet-like structures at the onset of mitosis, possibly by regulating homotypic membrane fusion. Belongs to the heat shock protein 70 family.

Heat shock protein 90; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. By stabilizing the receptor-type guanylate cyclase daf-11 or another sig [...]

GrpE protein homolog, mitochondrial; Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Seems to control the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins (By similarity).

T-complex protein 1 subunit alpha; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.

ATP-dependent Clp protease proteolytic subunit 1, mitochondrial; Clp cleaves peptides in various proteins in a process that requires ATP hydrolysis. Clp may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates; Belongs to the peptidase S14 family.

T-complex protein 1 subunit theta; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity). Required for correct subcellular localization of pgl-1; Belongs to the TCP-1 chaperonin family.

AFG3-like protein spg-7; Acts as a component of the m-AAA protease complex which is an ATP-dependent metalloprotease mediating degradation of non-assembled mitochondrial inner membrane proteins (By similarity). The complex is necessary for the assembly of mitochondrial respiratory chain and ATPase complexes (By similarity). Functions both in post-translational assembly and in the turnover of mistranslated or misfolded polypeptides. Plays a role in male tail tip morphogenesis. In the C-terminal section; belongs to the peptidase M41 family.

Stress activated transcription factor atfs-1; Acts as a transcription factor during mitochondrial stress by activating the mitochondrial unfolded protein response (mtUPR). Induces nuclear and mitochondrial gene transcription, including genes coding for mitochondrial chaperones and proteins involved in glycolysis, amino acid catabolism and innate immunity. Following mitochondrial stress, restores mitochondrial respiratory capacity by limiting the transcription of oxidative phosphorylation (OXPHOS) machinery genes and by promoting the assembly of OXPHOS complexes via the up-regulation of [...]