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Literature summary for 3.4.21.B57 extracted from
- Formation of the high-affinity calcium binding site in pro-subtilisin E with the insertion sequence IS1 of pro-Tk-subtilisin (2013), Biochemistry, 52, 9080-9088.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | bound at the high-affinity Ca1 site and low-affinity Ca2 site | Thermococcus kodakarensis |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermococcus kodakarensis | P58502 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | autocatalytic processing, pro-Tk-subtilisin from Thermococcus kodakarensis is fully folded, because it does not require the structural rearrangement upon autoprocessing for the formation of the Ca2+-binding Ca1 site due to the presence of the insertion sequence IS1 between the propeptide and subtilisin domains | Thermococcus kodakarensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Tk-subtilisin | - |
Thermococcus kodakarensis |
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