P26772
uniprot
P26772
canonical
amino_acid_sequence
MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGGKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD
uniprot
proteins
function
FUNCTION: Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. {ECO:0000250|UniProtKB:P61604}.
uniprot
proteins
mass_dalton
10902
uniprot
proteins
protein_family
GroES chaperonin family
uniprot
proteins
pubmed
1348860
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
7904573
uniprot
proteins
pubmed
8101099
uniprot
proteins
sequence_length
102
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P61604}.
uniprot
proteins