| IED ID | IndEnz0002007591 |
| Enzyme Type ID | protease007591 |
| Protein Name |
Protease PrsW EC 3.4.-.- Protease responsible for activating sigma-W Site-1 protease PrsW S1P protease PrsW |
| Gene Name | prsW ypdC BSU22940 |
| 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 | MFAIISAGIAPGIALLSYFYLKDQYDNEPVHMVLRSFFLGVVLVFPIMFIQYVLEKENVGGGSFFVSFLSSGFLEESLKWFILMISVYPHAHFDEHYDGIVYGASVSLGFATLENILYLIGHGVEHAFVRALLPVSCHALIGVIMGFYLGKARFSADKARVKWLTLSLVVPSLLHGSYDFILTALSNWIYYMLPFMVFLWWFGLRKAKKARSVNMMQV |
| Enzyme Length | 218 |
| Uniprot Accession Number | P50738 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor. Seems to be responsible for sensing antimicrobial peptides that damage the cell membrane and other agents that cause cell envelope stress. Therefore it is a protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in B.subtilis. {ECO:0000269|PubMed:16816000, ECO:0000269|PubMed:17020587, ECO:0000269|PubMed:19889088}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Frameshift (1); Mutagenesis (3); Site (3); Topological domain (5); Transmembrane (5) |
| Keywords | Cell membrane;Hydrolase;Membrane;Protease;Reference proteome;Transducer;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17020587}; Multi-pass membrane protein. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 24,719 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |