Cloned (Comment) | Organism |
---|---|
cloned in Escherichia coli, expression of ATPase and co-expression of the Hep1 in plasmids containing Ssc1 constructs | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Saccharomyces cerevisiae | 5739 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P0CS90 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + H2O + mitochondrial-protein[side 1] = ADP + phosphate + mitochondrial-protein[side 2] | the mitochondrial Hsp70 chaperone Ssc1 requires the Hsp70 escort protein Hep1, an L-shaped matrix protein with a zinc finger motif | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O | - |
Saccharomyces cerevisiae | ADP + phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | the ATPase and peptide binding domain (PBD) of Hsp70 proteins are connected by a linker segment that mediates communication between the domains. The minimal co-chaperone Hep1 binding entity of Ssc1 consists of the ATPase domain and the interdomain linker. The ATPase domain in combination with the interdomain linker is crucial for aggregation of Ssc1, stimulating the ATPase activity. In the absence of Hep1, the ATPase domain with the interdomain linker aggregated | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
mitochondrial Hsp70 chaperone Ssc1 | - |
Saccharomyces cerevisiae |
Ssc1 | - |
Saccharomyces cerevisiae |