| IED ID | IndEnz0002001914 |
| Enzyme Type ID | protease001914 |
| Protein Name |
Proteinase L5 EC 3.4.-.- Fragment |
| Gene Name | |
| Organism | Lysobacter sp. (strain XL1) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Lysobacter unclassified Lysobacter Lysobacter sp. (strain XL1) |
| Enzyme Sequence | ATVQGGIXYRMP |
| Enzyme Length | 12 |
| Uniprot Accession Number | P85158 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Peptidase. Has bacteriolytic activity. {ECO:0000269|Ref.1}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius. {ECO:0000269|Ref.1}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|Ref.1}; |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (1) |
| Keywords | Antibiotic;Antimicrobial;Bacteriolytic enzyme;Direct protein sequencing;Hydrolase;Protease;Secreted |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 1,304 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |