| IED ID | IndEnz0002002580 |
| Enzyme Type ID | protease002580 |
| Protein Name |
Peptidoglycan endopeptidase LytF EC 3.4.-.- Autolysin LytF Cell wall-associated polypeptide CWBP49' Gamma-D-glutamate-meso-diaminopimelate muropeptidase LytF Peptidoglycan hydrolase LytF Vegetative cell wall hydrolase LytF |
| Gene Name | lytF cwlE yhdD BSU09370 |
| 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 | MKKKLAAGLTASAIVGTTLVVTPAEAATIKVKSGDSLWKLAQTYNTSVAALTSANHLSTTVLSIGQTLTIPGSKSSTSSSTSSSTTKKSGSSVYTVKSGDSLWLIANEFKMTVQELKKLNGLSSDLIRAGQKLKVSGTVSSSSSSSKKSNSNKSSSSSSKSSSNKSSSSSSSTGTYKVQLGDSLWKIANKVNMSIAELKVLNNLKSDTIYVNQVLKTKSSGSDTSSKDNSSKSNQTSATTKYTVKSGDSLWKIANNYNLTVQQIRNINNLKSDVLYVGQVLKLTGKASSGSSSSSSSSSNASSGTTTTYTVKSGDSLWVIAQKFNVTAQQIREKNNLKTDVLQVGQKLVISGKASSSSSSGSSNTTSSTSAKINTMISAAKAQLGVPYRWGGTTPSGFDCSGFIYYVLNKVTSVSRLTAAGYWNTMKSVSQPAVGDFVFFSTYKAGPSHVGIYLGNGEFINANDSGVVISNMNNSYWKQRYLGAKRYF |
| Enzyme Length | 488 |
| Uniprot Accession Number | O07532 |
| Absorption | |
| Active Site | ACT_SITE 400; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284; ACT_SITE 449; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284; ACT_SITE 461; /evidence=ECO:0000255|PROSITE-ProRule:PRU01284 |
| Activity Regulation | ACTIVITY REGULATION: Is inhibited in vitro by para-hydroxymercuribenzoate, a sulfydryl inhibitor. {ECO:0000269|PubMed:10206711}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Cell wall hydrolase that cleaves gamma-D-glutamate-meso-diaminopimelate bonds in peptidoglycan. LytF is necessary and sufficient for vegetative daughter cell separation, and also seems to play a role in cell autolysis. {ECO:0000269|PubMed:10206711, ECO:0000269|PubMed:10322020, ECO:0000269|PubMed:19542270}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:10206711}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (6); Region (4); Sequence conflict (1); Signal peptide (1) |
| Keywords | Cell wall;Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Protease;Reference proteome;Repeat;Secreted;Signal;Thiol protease |
| Interact With | |
| Induction | INDUCTION: Expressed in the vegetative growth phase under exclusive control of sigma-D (SigD). Expression of lytF is heterogeneous in the exponentially growing cell population; it is ON in single cells and OFF in long chains. The same subpopulation of cells that express lytF also express flagellin. {ECO:0000269|PubMed:10206711, ECO:0000269|PubMed:10322020, ECO:0000269|PubMed:19542270}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10206711, ECO:0000269|PubMed:14594841}. Note=LytF is localized at cell separation sites and cell poles of rod-shaped cells during vegetative growth. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000269|PubMed:10206711 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 51,395 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |