| Accession | TIGR00714 |
| Name | hscB |
| Function | Fe-S protein assembly co-chaperone HscB |
| Gene Symbol | hscB |
| Trusted Cutoff | 46.75 |
| Domain Trusted Cutoff | 46.75 |
| Noise Cutoff | 44.70 |
| Domain Noise Cutoff | 44.70 |
| Isology Type | equivalog |
| HMM Length | 156 |
| Mainrole Category | Protein fate |
| Subrole Category | Protein folding and stabilization |
| Gene Ontology Term | GO:0005515: protein binding molecular_function |
| | GO:0006457: protein folding biological_process |
| Author | Haft DH |
| Entry Date | Feb 1 2000 10:52AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This HMM describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. |
| References | AL clustalw_manual
DR PFAM; PF00226; DnaJ
RN [1]
RM 99069337
RT The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system.
RA Silberg JJ, Hoff KG, Vickery LE
RL J Bacteriol 1998 Dec;180(24):6617-24
DR EXPERIMENTAL; EGAD|6265|EC2527; Escherichia coli
DR OUTGROUP; EGAD|155934|AA0494; Aquifex aeolicus
DR OUTGROUP; EGAD|163242|RP184
DR HAMAP; MF_00682; 109 of 111 |
| Genome Property | GenProp0138: iron-sulfur cluster assembly iscSUA-hscBA-fdx system (HMM) |
