EC Number   |
Natural Substrates |
|---|
  3.4.24.B23 | more |
regulation of SpoIVFB activity is achieved by a proteolytic cascade involving serine proteases, which are used as S1P protease in other S2P cascades. SpoIVB and CtpB are not involved in Site-1 cleavage of substrate but are required to relieve the inhibition of SpoIVFB by SpoIVFA and BofA |
| 3.4.24.B23 | pro-sigmaK + H2O |
involved in the sporulation process |
| 3.4.24.B23 | pro-sigmaK + H2O |
- |
| 3.4.24.B23 | pro-sigmaK + H2O |
maturation and activation of sigmaK by proteolytic removal of an N-terminal extension of 20 amino acids. Pro-sigmaK is associated with the outer forespore membrane with its N-terminal transmembrane segment, amino acids 1 to 27. Proteolytic cleavage by SpoIVFB releases the C-terminal sigmaK into the mother cell for directing transcription of genes involved in spore cortex and coat synthesis |
| 3.4.24.B23 | pro-sigmaK + H2O |
SpoIVFB protein and SpoIVFB protein with an extra transmembrane segment cleave membrane-tethered pro-sigmaK, releasing sigmaK to direct transcription of genes necessary for spore formation. The CBS domain of SpoIVFB interacts with pro-sugmaK, and ATP changes the interaction, suggesting that ATP regulates substrate access to the active site and renders cleavage sensitive to the cellular energy level |
| 3.4.24.B23 | pro-sigmaK + H2O |
cleavage site between S20 and Y21 |
