| IED ID | IndEnz0002008262 |
| Enzyme Type ID | protease008262 |
| Protein Name |
Anti-sigma-W factor RsiW Regulator of SigW Sigma-W anti-sigma factor RsiW |
| Gene Name | rsiW ybbM BSU01740 |
| 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 | MSCPEQIVQLMHMHLDGDILPKDEHVLNEHLETCEKCRKHFYEMEKSIALVRSTSHVEAPADFTANVMAKLPKEKKRASVKRWFRTHPVIAAAAVFIILMGGGFFNSWHNDHNFSVSKQPNLVVHNHTVTVPEGETVKGDVTVKNGKLIIKGKIDGDVTVVNGEKYMASAGQVTGQIEEINQLFDWTWYKMKSAGKSVLDAFNPNGEE |
| Enzyme Length | 208 |
| Uniprot Accession Number | Q45588 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: The anti-sigma factor for extracytoplasmic function (ECF) sigma factor sigma-W (SigW). Holds SigW, its cognate ECF sigma factor, in an inactive form until released by regulated intramembrane proteolysis (RIP). SigW and RsiW mediate cell response to cell wall stress (PubMed:12207695). RIP occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut periplasmically (site-1 protease, S1P, PrsW) (PubMed:16816000, PubMed:17020587), then within the membrane itself (site-2 protease, S2P, RasP) (PubMed:15130127), while cytoplasmic proteases finish degrading the anti-sigma factor, liberating sigma-W (PubMed:16899079). {ECO:0000269|PubMed:12207695, ECO:0000269|PubMed:15130127, ECO:0000269|PubMed:16816000, ECO:0000269|PubMed:16899079, ECO:0000269|PubMed:17020587, ECO:0000269|PubMed:21685450}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Frameshift (1); Helix (4); Metal binding (4); Mutagenesis (14); Topological domain (2); Transmembrane (1) |
| Keywords | 3D-structure;Cell membrane;Membrane;Metal-binding;Reference proteome;Stress response;Transcription;Transcription regulation;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | INDUCTION: By different stresses causing damage to the cell envelope, such as alkaline shock (PubMed:11454200), salt shock (PubMed:11544224), phage infection and certain antibiotics that affect cell wall biosynthesis (PubMed:12207695, PubMed:15870467). {ECO:0000269|PubMed:11454200, ECO:0000269|PubMed:11544224, ECO:0000269|PubMed:12207695, ECO:0000269|PubMed:15870467}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16899079}; Single-pass membrane protein {ECO:0000269|PubMed:16899079}. Note=Site-2 clipped RsiW is released from the membrane to the cytoplasm (PubMed:16899079). {ECO:0000269|PubMed:16899079}. |
| Modified Residue | |
| Post Translational Modification | PTM: Is processed by successive proteolytic events. First, the extracellular region of RsiW is cleaved by PrsW (site-1 cleavage) in response to cell envelope stresses (PubMed:16816000, PubMed:17020587). In a reconstituted E.coli system PrsW cuts between Ala-168 and Ser-169 followed by trimming by E.coli Tsp; the endogenous extracellular exopeptidase responsible for the event in B.subtilis has not been identified (PubMed:19889088). Next, it undergoes cleavage at an intramembrane site (site-2 cleavage) mediated by RasP (PubMed:15130127). This cleavage uncovers a cryptic proteolytic tag with conserved alanine residues in the transmembrane segment, that is recognized mainly by the ClpXP protease, which completely degrades the protein in the cytoplasm and leads to the induction of the sigma-W-controlled genes (PubMed:16899079). {ECO:0000269|PubMed:15130127, ECO:0000269|PubMed:16816000, ECO:0000269|PubMed:16899079, ECO:0000269|PubMed:17020587, ECO:0000269|PubMed:19889088}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5WUQ; 5WUR; |
| Mapped Pubmed ID | 14993308; |
| Motif | |
| Gene Encoded By | |
| Mass | 23,341 |
| Kinetics | |
| Metal Binding | METAL 3; /note=Zinc; /evidence=ECO:0000269|PubMed:28319136; METAL 30; /note=Zinc; via tele nitrogen; /evidence=ECO:0000269|PubMed:28319136; METAL 34; /note=Zinc; /evidence=ECO:0000269|PubMed:28319136; METAL 37; /note=Zinc; /evidence=ECO:0000269|PubMed:28319136 |
| Rhea ID | |
| Cross Reference Brenda |