| IED ID | IndEnz0002002583 |
| Enzyme Type ID | protease002583 |
| Protein Name |
Glycyl-glycine endopeptidase LytM EC 3.4.24.75 Autolysin LytM |
| Gene Name | lytM SAOUHSC_00248 |
| Organism | Staphylococcus aureus (strain NCTC 8325 / PS 47) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus aureus Staphylococcus aureus (strain NCTC 8325 / PS 47) |
| Enzyme Sequence | MKKLTAAAIATMGFATFTMAHQADAAETTNTQQAHTQMSTQSQDVSYGTYYTIDSNGDYHHTPDGNWNQAMFDNKEYSYTFVDAQGHTHYFYNCYPKNANANGSGQTYVNPATAGDNNDYTASQSQQHINQYGYQSNVGPDASYYSHSNNNQAYNSHDGNGKVNYPNGTSNQNGGSASKATASGHAKDASWLTSRKQLQPYGQYHGGGAHYGVDYAMPENSPVYSLTDGTVVQAGWSNYGGGNQVTIKEANSNNYQWYMHNNRLTVSAGDKVKAGDQIAYSGSTGNSTAPHVHFQRMSGGIGNQYAVDPTSYLQSR |
| Enzyme Length | 316 |
| Uniprot Accession Number | O33599 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by DEPC, HgCl(2), ammonium sulfate and glucosamine. Inhibited by 1,10-phenanthroline at concentrations as low as 1 mM. Glycine hydroxamate, Zn(2+), Hg(2+) and EDTA inhibit the activity at 10 mM. Sodium chloride (NaCl) and potassium chloride (KCl) inhibit protease activity at 100 mM. {ECO:0000269|PubMed:10220159}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans.; EC=3.4.24.75; |
| DNA Binding | |
| EC Number | 3.4.24.75 |
| Enzyme Function | FUNCTION: Peptidoglycan hydrolase (autolysin) specifically acting on polyglycine interpeptide bridges of the cell wall peptidoglycan. {ECO:0000269|PubMed:10220159, ECO:0000269|PubMed:8095258}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable at 100 degrees Celsius for 15 minutes, but loses activity at the same temperature within 30 minutes. {ECO:0000269|PubMed:10220159}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-8. {ECO:0000269|PubMed:10220159}; |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (14); Chain (1); Compositional bias (1); Erroneous initiation (1); Helix (6); Metal binding (4); Mutagenesis (5); Region (1); Sequence conflict (2); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Cell wall biogenesis/degradation;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Virulence;Zinc;Zymogen |
| Interact With | |
| Induction | INDUCTION: Repressed by MgrA. More protein is secreted in a double secG/secY2 mutant (at protein level). {ECO:0000269|PubMed:20472795}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10220159, ECO:0000269|PubMed:20472795}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000269|PubMed:9171409 |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 1QWY; 2B0P; 2B13; 2B44; 4ZYB; |
| Mapped Pubmed ID | 16269153; 26437833; |
| Motif | |
| Gene Encoded By | |
| Mass | 34,317 |
| Kinetics | |
| Metal Binding | METAL 117; /note="Zinc"; /evidence="ECO:0000269|PubMed:14687573, ECO:0007744|PDB:1QWY"; METAL 210; /note="Zinc; via tele nitrogen"; /evidence="ECO:0000269|PubMed:14687573, ECO:0007744|PDB:1QWY"; METAL 214; /note="Zinc"; /evidence="ECO:0000269|PubMed:14687573, ECO:0007744|PDB:1QWY"; METAL 293; /note="Zinc; via pros nitrogen"; /evidence="ECO:0000269|PubMed:14687573, ECO:0007744|PDB:1QWY" |
| Rhea ID | |
| Cross Reference Brenda |