SpoIVB peptidase
| SpoIVB peptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.21.116 | ||||||||
| CAS no. | 296241-18-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
SpoIVB peptidase (EC 3.4.21.116, sporulation factor IV B protease) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction
- Self-cleaves Val52-Asn53, Ala62-Phe63 and Val74-Thr75 at the N-terminus of SpoIVB
This enzyme participates in gene expression during the later stages of spore formation in Bacillus subtilis.
References
- ^ Wakeley, P.R.; Dorazi, R.; Hoa, N.T.; Bowyer, J.R.; Cutting, S.M. (2000). "Proteolysis of SpolVB is a critical determinant in signalling of pro-σK processing in Bacillus subtilis". Mol. Microbiol. 36: 1336–1348. doi:10.1046/j.1365-2958.2000.01946.x. PMID 10931284.
- ^ Hoa, N.T.; Brannigan, J.A.; Cutting, S.M. (2001). "The PDZ domain of the SpoIVB serine peptidase facilitates multiple functions". J. Bacteriol. 183: 4364–4373. doi:10.1128/jb.183.14.4364-4373.2001. PMC 95327. PMID 11418578.
- ^ Hoa, N.T.; Brannigan, J.A.; Cutting, S.M. (2002). "The Bacillus subtilis signaling protein SpoIVB defines a new family of serine peptidases". J. Bacteriol. 184: 191–199. doi:10.1128/jb.184.1.191-199.2002. PMC 134772. PMID 11741860.
- ^ Dong, T.C.; Cutting, S.M. (2003). "SpoIVB-mediated cleavage of SpoIVFA could provide the intercellular signal to activate processing of pro-σK in Bacillus subtilis". Mol. Microbiol. 49: 1425–1434. doi:10.1046/j.1365-2958.2003.03651.x. PMID 12940997.
External links
- SpoIVB+peptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)