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; |