| IED ID | IndEnz0002009482 |
| Enzyme Type ID | protease009482 |
| Protein Name |
SpoIVB peptidase EC 3.4.21.116 Sporulation factor IV B protease Stage IV sporulation protein B Cleaved into: SpoIVB peptidase 45 kDa isoform; SpoIVB peptidase 43 kDa isoform; SpoIVB peptidase 42 kDa isoform |
| Gene Name | spoIVB BSU24230 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MPDNIRKAVGLILLVSLLSVGLCKPLKEYLLIPTQMRVFETQTQAIETSLSVNAQTSESSEAFTVKKDPHEIKVTGKKSGESELVYDLAGFPIKKTKVHVLPDLKVIPGGQSIGVKLHSVGVLVVGFHQINTSEGKKSPGETAGIEAGDIIIEMNGQKIEKMNDVAPFIQKAGKTGESLDLLIKRDKQKIKTKLIPEKDEGEGKYRIGLYIRDSAAGIGTMTFYEPKTKKYGALGHVISDMDTKKPIVVENGEIVKSTVTSIEKGTGGNPGEKLARFSSERKTIGDINRNSPFGIFGTLHQPIQNNISDQALPVAFSTEVKKGPAEILTVIDDDKVEKFDIEIVSTTPQKFPATKGMVLKITDPRLLKETGGIVQGMSGSPIIQNGKVIGAVTHVFVNDPTSGYGVHIEWMLSEAGIDIYGKEKAS |
| Enzyme Length | 426 |
| Uniprot Accession Number | P17896 |
| Absorption | |
| Active Site | ACT_SITE 236; /note=Charge relay system; /evidence=ECO:0000305; ACT_SITE 363; /note=Charge relay system; /evidence=ECO:0000305; ACT_SITE 378; /note=Charge relay system; /evidence=ECO:0000305 |
| Activity Regulation | ACTIVITY REGULATION: The zymogen is inhibited from undergoing autoactivation by BofC. The protease is inactivated by proteolytic cleavage. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Self-cleaves 52-Val-|-Asn-53, 62-Ala-|-Phe-63 and 74-Val-|-Thr-75 at the N-terminus of SpoIVB.; EC=3.4.21.116; |
| DNA Binding | |
| EC Number | 3.4.21.116 |
| Enzyme Function | FUNCTION: 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. {ECO:0000269|PubMed:10931284, ECO:0000269|PubMed:11741860}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (3); Domain (2); Mutagenesis (15); Propeptide (1); Region (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Direct protein sequencing;Hydrolase;Protease;Reference proteome;Serine protease;Signal;Sporulation;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Forespore intermembrane space. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 24243021; |
| Motif | |
| Gene Encoded By | |
| Mass | 46,075 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.116; |