Co-chaperone HscB, C-terminal oligomerisation domain (IPR009073)

Short name: HscB_oligo_C

Overlapping homologous superfamilies

Domain relationships



This entry represents the C-terminal oligomerisation domain found in HscB (heat shock cognate protein B), which is also known as HSC20 (20K heat shock cognate protein) and J-protein Jac1 in yeast mitochondria [PMID: 22306468]. HscB acts as a co-chaperone to regulate the ATPase activity and peptide-binding specificity of the molecular chaperone HscA, also known as HSC66 (HSP70 class). HscB proteins contain two domains, an N-terminal J-domain, which is involved in interactions with HscA, connected by a short loop to the C-terminal oligomerisation domain; the two domains make contact through a hydrophobic interface. The core of the oligomerisation domain is thought to bind and target proteins to HscA and consists of an open, three-helical bundle [PMID: 11124030]. HscB, along with HscA, has been shown to play a role in the biogenesis of iron-sulphur proteins.

GO terms

Biological Process

GO:0051259 protein complex oligomerization

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.