Detail Information for IndEnz0002001019
IED ID IndEnz0002001019
Enzyme Type ID protease001019
Protein Name Subtilisin BPN'
EC 3.4.21.62
Alkaline protease
Subtilisin DFE
Subtilisin Novo
Gene Name apr
Organism Bacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus amyloliquefaciens group Bacillus amyloliquefaciens (Bacillus velezensis)
Enzyme Sequence MRGKKVWISLLFALALIFTMAFGSTSSAQAAGKSNGEKKYIVGFKQTMSTMSAAKKKDVISEKGGKVQKQFKYVDAASATLNEKAVKELKKDPSVAYVEEDHVAHAYAQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQDNNSHGTHVAGTVAALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENTTTKLGDSFYYGKGLINVQAAAQ
Enzyme Length 382
Uniprot Accession Number P00782
Absorption
Active Site ACT_SITE 139; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818"; ACT_SITE 171; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818"; ACT_SITE 328; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:5249818"
Activity Regulation ACTIVITY REGULATION: Completely inhibited by phenylmethylsulfony fluoride (PMSF) and partially inhibited by benzamidine hydrochloride, leupeptin, and pepstatin A. {ECO:0000269|PubMed:12524032}.
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. Has a high substrate specificity to fibrin. {ECO:0000269|PubMed:12524032}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 48 degrees Celsius. {ECO:0000269|PubMed:12524032};
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:12524032};
Pathway
nucleotide Binding
Features Active site (3); Beta strand (22); Chain (1); Domain (2); Erroneous initiation (1); Helix (12); Metal binding (9); Natural variant (1); Propeptide (1); Signal peptide (1); Turn (4)
Keywords 3D-structure;Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Secreted;Serine protease;Signal;Sporulation;Zymogen
Interact With Q40059
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..30; /evidence=ECO:0000250
Structure 3D X-ray crystallography (63)
Cross Reference PDB 1A2Q; 1AK9; 1AQN; 1AU9; 1DUI; 1GNS; 1GNV; 1LW6; 1S01; 1S02; 1SBH; 1SBI; 1SBN; 1SBT; 1SIB; 1SPB; 1ST2; 1SUA; 1SUB; 1SUC; 1SUD; 1SUE; 1SUP; 1TM1; 1TM3; 1TM4; 1TM5; 1TM7; 1TMG; 1TO1; 1TO2; 1UBN; 1V5I; 1Y1K; 1Y33; 1Y34; 1Y3B; 1Y3C; 1Y3D; 1Y3F; 1Y48; 1Y4A; 1Y4D; 1YJA; 1YJB; 1YJC; 2SBT; 2SIC; 2SNI; 2ST1; 3BGO; 3CNQ; 3CO0; 3F49; 3SIC; 5OX2; 5SIC; 7AM3; 7AM4; 7AM5; 7AM6; 7AM7; 7AM8;
Mapped Pubmed ID 10048334; 10350485; 12011071; 12142461; 15504027; 15865427; 18507395; 1891457; 1920411; 19761257; 1992167; 2127106; 29300408; 3064813; 3286644; 33717424; 4508127; 5160720; 8332608; 8535784; 9552156;
Motif
Gene Encoded By
Mass 39,181
Kinetics
Metal Binding METAL 109; /note=Calcium 1; METAL 148; /note=Calcium 1; METAL 182; /note=Calcium 1; via carbonyl oxygen; METAL 184; /note=Calcium 1; METAL 186; /note=Calcium 1; via carbonyl oxygen; METAL 188; /note=Calcium 1; via carbonyl oxygen; METAL 276; /note=Calcium 2; via carbonyl oxygen; METAL 278; /note=Calcium 2; via carbonyl oxygen; METAL 281; /note=Calcium 2; via carbonyl oxygen
Rhea ID
Cross Reference Brenda 3.4.21.62;