| IED ID | IndEnz0002002577 |
| Enzyme Type ID | protease002577 |
| Protein Name |
D-alanyl-L-alanine endopeptidase EC 3.4.22.- 1,4-N-acetylmuramidase EC 3.2.1.17 B30 lysin Endoysin Glycosidase |
| Gene Name | |
| Organism | Streptococcus phage B30 (Streptococcus agalactiae bacteriophage B30) |
| Taxonomic Lineage | Viruses Duplodnaviria Heunggongvirae Uroviricota Caudoviricetes Caudovirales unclassified Caudovirales Streptococcus phage B30 (Streptococcus agalactiae bacteriophage B30) |
| Enzyme Sequence | MATYQEYKSRSNGNAYDIDGSFGAQCWDGYADYCKYLGLPYANCTNTGYARDIWEQRHENGILNYFDEVEVMQAGDVAIFMVVDGVTPYSHVAIFDSDAGGGYGWFLGQNQGGANGAYNLVKIPYSATYPTAFRPKSFKNAVTVTDNTGLNKGDYFIDVSAYQQADLTTTCQQAGTTKTIIKVSESIAWLSDRHQQQANTSDPIGYYHFGRFGGDSALAQREADLFLSNLPSKKVSYLVIDYEDSASADKQANTNAVIAFMDKIASAGYKPIYYSYKPFTLNNIDYQKIIAKYPNSIWIAGYPDYEVRTEPLWEFFPSMDGVRWWQFTSVGVAGGLDKNIVLLADDSSKMDIPKVDKPQELTFYQKLATNTKLDNSNVPYYEATLSTDYYVESKPNASSADKEFIKAGTRVRVYEKVNGWSRINHPESAQWVEDNYLVNATDM |
| Enzyme Length | 443 |
| Uniprot Accession Number | Q8HA43 |
| Absorption | |
| Active Site | ACT_SITE 26; /note=Nucleophile; /evidence=ECO:0000305|PubMed:15256551; ACT_SITE 91; /note=Increases nucleophilicity of active site cys; for D-alanyl-L-alanine endopeptidase activity; /evidence=ECO:0000305|PubMed:15256551 |
| Activity Regulation | ACTIVITY REGULATION: Ca++ enhances the activity of the enzyme. {ECO:0000269|PubMed:15256551}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; Evidence={ECO:0000269|PubMed:17021237}; |
| DNA Binding | |
| EC Number | 3.4.22.-; 3.2.1.17 |
| Enzyme Function | FUNCTION: The endopeptidase activity cleaves the bacterial peptidoglycan between D-alanine and L-alanine (PubMed:15256551, PubMed:17021237). The N-acetyl-muramidase activity cleaves between N-acetylmuramic acid and N-acetylglucosamine bonds (PubMed:17021237). {ECO:0000269|PubMed:15256551, ECO:0000269|PubMed:17021237}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:15256551}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (2); Mutagenesis (6); Region (1); Site (2) |
| Keywords | Antimicrobial;Bacteriolytic enzyme;Glycosidase;Hydrolase;Multifunctional enzyme;Protease |
| 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 | 49,672 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |