| IED ID | IndEnz0002001568 |
| Enzyme Type ID | protease001568 |
| Protein Name |
Subtilisin E EC 3.4.21.62 |
| Gene Name | aprE apr aprA sprE BSU10300 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MRSKKLWISLLFALTLIFTMAFSNMSAQAAGKSSTEKKYIVGFKQTMSAMSSAKKKDVISEKGGKVQKQFKYVNAAAATLDEKAVKELKKDPSVAYVEEDHIAHEYAQSVPYGISQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLNVRGGASFVPSETNPYQDGSSHGTHVAGTIAALNNSIGVLGVAPSASLYAVKVLDSTGSGQYSWIINGIEWAISNNMDVINMSLGGPTGSTALKTVVDKAVSSGIVVAAAAGNEGSSGSTSTVGYPAKYPSTIAVGAVNSSNQRASFSSAGSELDVMAPGVSIQSTLPGGTYGAYNGTSMATPHVAGAAALILSKHPTWTNAQVRDRLESTATYLGNSFYYGKGLINVQAAAQ |
| Enzyme Length | 381 |
| Uniprot Accession Number | P04189 |
| Absorption | |
| Active Site | ACT_SITE 138; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:9811547"; ACT_SITE 170; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:9811547"; ACT_SITE 327; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:9811547" |
| 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 (19); Chain (1); Domain (2); Helix (11); Metal binding (10); Mutagenesis (1); Propeptide (1); Sequence conflict (4); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Autocatalytic cleavage;Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Protease;Reference proteome;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:0000269|PubMed:3090033 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1SCJ; 3WHI; 6O44; 6PAK; |
| Mapped Pubmed ID | 24279884; 30914195; 31615894; |
| Motif | |
| Gene Encoded By | |
| Mass | 39,479 |
| Kinetics | |
| Metal Binding | METAL 108; /note=Calcium 1; /evidence=ECO:0000269|PubMed:9811547; METAL 147; /note=Calcium 1; /evidence=ECO:0000269|PubMed:9811547; METAL 181; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:9811547; METAL 183; /note=Calcium 1; /evidence=ECO:0000269|PubMed:9811547; METAL 185; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:9811547; METAL 187; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:9811547; METAL 275; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:9811547; METAL 277; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:9811547; METAL 280; /note=Calcium 2; /evidence=ECO:0000269|PubMed:9811547; METAL 303; /note=Calcium 2; /evidence=ECO:0000269|PubMed:9811547 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.62; |