| IED ID | IndEnz0002008225 |
| Enzyme Type ID | protease008225 |
| Protein Name |
ECF RNA polymerase sigma factor SigW ECF sigma factor SigW Alternative RNA polymerase sigma factor SigW RNA polymerase sigma-W factor Sigma-W factor |
| Gene Name | sigW ybbL BSU01730 |
| 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 | MEMMIKKRIKQVKKGDQDAFADIVDIYKDKIYQLCYRMLGNVHEAEDIAQEAFIRAYVNIDSFDINRKFSTWLYRIATNLTIDRIRKKKPDYYLDAEVAGTEGLTMYSQIVADGVLPEDAVVSLELSNTIQQKILKLPDKYRTVIVLKYIDELSLIEIGEILNIPVGTVKTRIHRGREALRKQLRDL |
| Enzyme Length | 187 |
| Uniprot Accession Number | Q45585 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Extracytoplasmic function (ECF) sigma factors are held in an inactive form by a cognate anti-sigma factor (RsiW for this protein) until released by regulated membrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal (envelope stress) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The anti-sigma factor RsiW is a membrane protein, binding sigma-W in the cytoplasm. RsiW is first cut extracytoplasmically (site-1 protease, S1P, by PrsW) (PubMed:16816000), then within the membrane itself (site-2 protease, S2P, by RasP) (PubMed:15130127), while cytoplasmic proteases (predominantly ClpX-ClpP) finish degrading the regulatory protein, liberating sigma-W (PubMed:16899079). {ECO:0000269|PubMed:15130127, ECO:0000269|PubMed:16816000, ECO:0000269|PubMed:16899079}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | DNA_BIND 166..184; /note=H-T-H motif; /evidence=ECO:0000305|PubMed:28319136 |
| EC Number | |
| Enzyme Function | FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Sigma-W controls genes involved in response to cell envelope stress such as antimicrobial peptides (PubMed:12207695, PubMed:15870467), alkaline pH (PubMed:11454200), transport processes and detoxification. {ECO:0000269|PubMed:11454200, ECO:0000269|PubMed:12207695, ECO:0000269|PubMed:15870467, ECO:0000269|PubMed:21685450, ECO:0000305|PubMed:21710567}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); DNA binding (1); Helix (10); Motif (1); Region (2) |
| Keywords | 3D-structure;DNA-binding;Reference proteome;Sigma factor;Stress response;Transcription;Transcription regulation |
| 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). Does not respond to oxidative stress caused by diamide (PubMed:21685450). Association with RNAP core increases during most stresses but not during sporulation (at protein level) (PubMed:21710567). {ECO:0000269|PubMed:11454200, ECO:0000269|PubMed:11544224, ECO:0000269|PubMed:12207695, ECO:0000269|PubMed:15870467, ECO:0000269|PubMed:21685450, ECO:0000269|PubMed:21710567}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 5WUQ; 5WUR; 6JHE; |
| Mapped Pubmed ID | 14993308; 25374563; 31461489; |
| Motif | MOTIF 47..50; /note=Polymerase core binding |
| Gene Encoded By | |
| Mass | 21,713 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |