| IED ID | IndEnz0002009419 |
| Enzyme Type ID | protease009419 |
| Protein Name |
Subtilisin J EC 3.4.21.62 |
| Gene Name | aprJ |
| Organism | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Geobacillus Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Enzyme Sequence | MRSKKLWISLLFALTLIFTMAFSNMSVQAAGKSSTEKKYIVGFKQTMSAMSSAKKKDVISEKGGKVQKQFKYVNAAAATLDEKAVKELKKDPSVAYVEEDHIAHEYAQSVPYGISQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLNVRGGASFVPSETNPYQDGSSHGTHVAGTIAALNNSIGVLGVSPSASLYAVKVLDSTGSGQYSWIINGIEWAISNNMDVINMSLGGPSGSTALKTVVDKAVSSGIVVAAAAGNEGSSGSSSTVGYPAKYPSTIAVGAVNSSNQRASFSSAGSELDVMAPGVSIQSTLPGGTYGAYNGTSMATPHVAGAAALILSKHPTWTNAQVRDRLESTATYLGNSFYYGKGLINVQAAAQ |
| Enzyme Length | 381 |
| Uniprot Accession Number | P29142 |
| Absorption | |
| Active Site | ACT_SITE 138; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 170; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 327; /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); Chain (1); Domain (2); Metal binding (9); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Hydrolase;Metal-binding;Protease;Secreted;Serine protease;Signal;Sporulation;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..29; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 39,495 |
| Kinetics | |
| Metal Binding | METAL 108; /note=Calcium 1; /evidence=ECO:0000250; METAL 147; /note=Calcium 1; /evidence=ECO:0000250; METAL 181; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 183; /note=Calcium 1; /evidence=ECO:0000250; METAL 185; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 187; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 275; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 277; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 280; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |