| EC |
3.4.21.116 |
| Accepted name: |
SpoIVB peptidase |
| Reaction: |
Self-cleaves Val52┼Asn53, Ala62┼Phe63 and Val74┼Thr75 at the N-terminus of SpoIVB |
| Other name(s): |
sporulation factor IV B protease |
| Comments: |
This enzyme plays a central role in a regulatory checkpoint (the σK checkpoint), which coordinates gene expression during the later stages of spore formation in Bacillus subtilis [1,3]. The enzyme activates proteolytic processing of a sporulation-specific sigma factor, pro-σK, to its mature and active form, σK, by self-cleavage [1,3]. The enzyme is also subject to secondary proteolysis, which presumably inactivates SpoIVB [3]. The enzyme is also essential for the formation of heat-resistant spores. Belongs in peptidase family S55. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 296241-18-4 |
| References: |
| 1. |
Wakeley, P.R., Dorazi, R., Hoa, N.T., Bowyer, J.R. and Cutting, S.M. Proteolysis of SpolVB is a critical determinant in signalling of pro-σK processing in Bacillus subtilis. Mol. Microbiol. 36 (2000) 1336–1348. [DOI] [PMID: 10931284] |
| 2. |
Hoa, N.T., Brannigan, J.A. and Cutting, S.M. The PDZ domain of the SpoIVB serine peptidase facilitates multiple functions. J. Bacteriol. 183 (2001) 4364–4373. [DOI] [PMID: 11418578] |
| 3. |
Hoa, N.T., Brannigan, J.A. and Cutting, S.M. The Bacillus subtilis signaling protein SpoIVB defines a new family of serine peptidases. J. Bacteriol. 184 (2002) 191–199. [DOI] [PMID: 11741860] |
| 4. |
Dong, T.C. and Cutting, S.M. SpoIVB-mediated cleavage of SpoIVFA could provide the intercellular signal to activate processing of pro-σK in Bacillus subtilis. Mol. Microbiol. 49 (2003) 1425–1434. [DOI] [PMID: 12940997] |
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| [EC 3.4.21.116 created 2006] |
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