| Primary Identifier | IPR004640 | Type | Family |
| Short Name | HscB |
| description | The final step of iron-sulfur protein assembly involves transfer of an iron-sulfur cluster from a cluster-donor to a cluster-acceptor protein []. 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) []. The co-chaperone HscB recruits the scaffold protein for Fe-S cluster biogenesis Isu1/IscU, guiding it to the chaperone HscA [, ], and enhances the intrinsic ATPase activity of the HscA []. |
