IED ID | IndEnz0002014012 |
Enzyme Type ID | protease014012 |
Protein Name |
Glycyl-glycine endopeptidase ALE-1 EC 3.4.24.75 Staphylolytic enzyme ALE-1 |
Gene Name | |
Organism | Staphylococcus capitis |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Staphylococcaceae Staphylococcus Staphylococcus capitis |
Enzyme Sequence | MDTNRKFTLVKSLSIGLGTFLVGSVFLTVNDEASASTKVDAPKVEQEAPAKADAPKVEQEAPAKADAPKVEQEAPAKVDAPKVEQEAPAKVDAPKVEQEAPAKADAPKVEQKRTFVREAAQSNHSASWLNNYKKGYGYGPYPLGINGGNHYGVDFFMNVGTPVRAISDGKIVEAGWTNYGGGNEIGLVENDGVHRQWYMHLSKFNVKVGDRVKAGQIIGWSGSTGYSTAPHLHFQRMTNSFSNNTAQDPMPFLKSAGYGSNSTSSSNNNGYKTNKYGTLYKSESASFTANTDIITRLTGPFRSMPQSGVLRKGLTIKYDEVMKQDGHVWVGYNTNSGKRVYLPVRTWNESTGELGPLWGTIK |
Enzyme Length | 362 |
Uniprot Accession Number | O05156 |
Absorption | |
Active Site | ACT_SITE 231; /evidence=ECO:0000250 |
Activity Regulation | |
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: Lyses staphylococcal cells by hydrolyzing the polyglycine interpeptide bridges of the peptidoglycan. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-9.; |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Beta strand (7); Chain (1); Compositional bias (1); Domain (1); Metal binding (3); Region (1); Signal peptide (1); Turn (1) |
Keywords | 3D-structure;Cell wall biogenesis/degradation;Hydrolase;Metal-binding;Metalloprotease;Protease;Repeat;Secreted;Signal;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..35 |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1R77; |
Mapped Pubmed ID | 16257954; |
Motif | |
Gene Encoded By | |
Mass | 39,350 |
Kinetics | |
Metal Binding | METAL 150; /note=Zinc; /evidence=ECO:0000305; METAL 154; /note=Zinc; /evidence=ECO:0000305; METAL 233; /note=Zinc; /evidence=ECO:0000305 |
Rhea ID | |
Cross Reference Brenda |