Co-chaperone Hsc20 (IPR004640)

Short name: HscB

Overlapping homologous superfamilies


Family relationships



The final step of iron-sulfur protein assembly involves transfer of an iron-sulfur cluster from a cluster-donor to a cluster-acceptor protein [PMID: 12970193]. This process is facilitated by a specialized chaperone system, which consists of a molecular chaperone from the Hsc70 family, HscA in E. coli, and a co-chaperone of the J-domain family, Hsc20/HscB (known as Jac1 in fungi) [PMID: 16964969]. The co-chaperone HscB recruits the scaffold protein for Fe-S cluster biogenesis Isu1/IscU, guiding it to the chaperone HscA [PMID: 16551614, PMID: 22306468], and enhances the intrinsic ATPase activity of the HscA [PMID: 15485839].

GO terms

Biological Process

GO:0097428 protein maturation by iron-sulfur cluster transfer

Molecular Function

GO:0001671 ATPase activator activity
GO:0051087 chaperone binding

Cellular Component

No terms assigned in this category.

Contributing signatures

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