Structural highlights
Function
SP4B_BACSU Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then cleaves the C-terminus of the SpoIVFA metalloprotease activating the latter.[1] [2]
References
- ↑ Wakeley PR, Dorazi R, Hoa NT, Bowyer JR, Cutting SM. Proteolysis of SpolVB is a critical determinant in signalling of Pro-sigmaK processing in Bacillus subtilis. Mol Microbiol. 2000 Jun;36(6):1336-48. PMID:10931284 doi:10.1046/j.1365-2958.2000.01946.x
- ↑ Hoa NT, Brannigan JA, Cutting SM. The Bacillus subtilis signaling protein SpoIVB defines a new family of serine peptidases. J Bacteriol. 2002 Jan;184(1):191-9. PMID:11741860 doi:10.1128/JB.184.1.191-199.2002