| IED ID | IndEnz0010001398 |
| Enzyme Type ID | esterase001398 |
| Protein Name |
Phospholipase YtpA EC 3.1.1.- Bacilysocin biosynthesis protein YtpA |
| Gene Name | ytpA BSU30510 |
| 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 | MWTWKADRPVAVIVIIHGASEYHGRYKWLIEMWRSSGYHVVMGDLPGQGTTTRARGHIRSFQEYIDEVDAWIDKARTFDLPVFLLGHSMGGLVAIEWVKQQRNPRITGIILSSPCLGLQIKVNKALDLASKGLNVIAPSLKVDSGLSIDMATRNEDVIEADQNDSLYVRKVSVRWYRELLKTIESAMVPTEAFLKVPLLVMQAGDDKLVDKTMVIKWFNGVASHNKAYREWEGLYHEIFNEPEREDVFKAARAFTDQYI |
| Enzyme Length | 259 |
| Uniprot Accession Number | O34705 |
| Absorption | |
| Active Site | ACT_SITE 88; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 206; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037; ACT_SITE 236; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10037 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.1.1.- |
| Enzyme Function | FUNCTION: Phospholipase involved in the biosynthesis of the antibiotic bacilysocin. It probably catalyzes the hydrolysis of the 2-sn-acyl moiety of phosphatidylglycerol to produce bacilysocin (lysophosphatidylglycerol). Is also able to catalyze the hydrolysis reaction of one acyl bond in phosphatidylcholine in vitro (actual cleavage point is unknown), resulting in lysophosphatidylcholine. {ECO:0000269|PubMed:11796336}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Antibiotic biosynthesis; bacilysocin biosynthesis. {ECO:0000269|PubMed:11796336}. |
| nucleotide Binding | |
| Features | Active site (3); Chain (1) |
| Keywords | Antibiotic biosynthesis;Hydrolase;Reference proteome;Serine esterase |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 29,566 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |