IED ID | IndEnz0002001016 |
Enzyme Type ID | protease001016 |
Protein Name |
Subtilisin BL EC 3.4.21.62 Alkaline protease |
Gene Name | |
Organism | Lederbergia lentus (Bacillus lentus) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Lederbergia Lederbergia lentus (Bacillus lentus) |
Enzyme Sequence | AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGNGHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGADGRGAISSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGASSISYPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQIRNHLKNTATSLGSTNLYGSGLVNAEAATR |
Enzyme Length | 269 |
Uniprot Accession Number | P29599 |
Absorption | |
Active Site | ACT_SITE 32; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 62; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 215; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; |
DNA Binding | |
EC Number | 3.4.21.62 |
Enzyme Function | FUNCTION: Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Beta strand (13); Chain (1); Domain (1); Helix (9); Metal binding (9); Turn (2) |
Keywords | 3D-structure;Calcium;Hydrolase;Metal-binding;Protease;Secreted;Serine protease;Sporulation |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 1ST3; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 26,824 |
Kinetics | |
Metal Binding | METAL 2; /note=Calcium 1; METAL 40; /note=Calcium 1; METAL 73; /note=Calcium 1; via carbonyl oxygen; METAL 75; /note=Calcium 1; METAL 77; /note=Calcium 1; via carbonyl oxygen; METAL 79; /note=Calcium 1; via carbonyl oxygen; METAL 163; /note=Calcium 2; via carbonyl oxygen; METAL 165; /note=Calcium 2; via carbonyl oxygen; METAL 168; /note=Calcium 2; via carbonyl oxygen |
Rhea ID | |
Cross Reference Brenda |