| IED ID | IndEnz0005000712 |
| Enzyme Type ID | lipase000712 |
| Protein Name |
Sporulation killing factor SKF Sporulation-killing factor SkfA |
| Gene Name | skfA ybcO BSU01910 |
| 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 | MKRNQKEWESVSKKGLMKPGGTSIVKAAGCMGCWASKSIAMTRVCALPHPAMRAI |
| Enzyme Length | 55 |
| Uniprot Accession Number | O31422 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Produces a 26-residue extracellular sporulation filling factor (SKF) that induces the lysis of other B.subtilis cells that have not entered the sporulation pathway, providing a source of nutrients to support sporulation, and at the same time delaying commitment to the energetically expensive and irreversible onset of sporulation (PubMed:12817086, PubMed:20805502). Can also inhibit growth of other bacteria at high concentrations (PubMed:11851812). Addition of SKF to solid cultures induces killing, but it is much less effective than SDP (AC O34344) (PubMed:20805502). Has a role in protecting the secreted lipase LipA against proteolysis, either by modulating its folding or by acting as a protease inhibitor (PubMed:15812018). {ECO:0000269|PubMed:11851812, ECO:0000269|PubMed:12817086, ECO:0000269|PubMed:15812018, ECO:0000269|PubMed:20805502}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Cross-link (2); Disulfide bond (1); Mutagenesis (6); Peptide (1); Propeptide (1) |
| Keywords | Antibiotic;Antimicrobial;Bacteriocin;Direct protein sequencing;Disulfide bond;Reference proteome;Secreted;Thioether bond |
| Interact With | |
| Induction | INDUCTION: By Spo0A (PubMed:12817086) and PhoP (PubMed:16816204), during nutrient starvation, especially phosphate starvation. Repressed by AbrB during normal growth when nutrients are plentiful, in association with the transcriptional repressor Abh. {ECO:0000269|PubMed:12817086, ECO:0000269|PubMed:15687200, ECO:0000269|PubMed:16816204, ECO:0000269|PubMed:17720793}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20805502}. Note=Probably secreted by the ABC transporter SkfEF. {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: This is a cyclic peptide (PubMed:20805502, PubMed:23282011). The first step in SKF maturation is probably thioether bond formation (PubMed:23282011). {ECO:0000269|PubMed:20805502, ECO:0000269|PubMed:23282011}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 5,934 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |