Detail Information for IndEnz0002001016
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