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Literature summary extracted from
- Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export (2006), Protein Sci., 15, 1379-1386.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.4.2.5 | Escherichia coli | - |
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- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.4.2.5 | ATP + H2O | SecB, a small cytosolic chaperone, captures the precursor polypeptides before they fold and delivers them to the membrane translocon through interactions with SecA. Both SecB and SecA display twofold symmetry and yet the complex between the two is stabilized by contacts that are distributed asymmetrically | Escherichia coli | ADP + phosphate | - |
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