| IED ID | IndEnz0002015655 |
| Enzyme Type ID | protease015655 |
| Protein Name |
Bacillolysin EC 3.4.24.28 Neutral protease |
| Gene Name | npr |
| 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 | MGLGKKLSVAVAASFMSLTISLPGVQAAENPQLKENLTNFVPKHSLVQSELPSVSDKAIKQYLKQNGKVFKGNPSERLKLIDQTTDDLGYKHFRYVPVVNGVPVKDSQVIIHVDKSNNVYAINGELNNDVSAKTANSKKLSANQALDHAYKAIGKSPEAVSNGTVANKNKAELKAAATKDGKYRLAYDVTIRYIEPEPANWEVTVDAETGKILKKQNKVEHAATTGTGTTLKGKTVSLNISSESGKYVLRDLSKPTGTQIITYDLQNREYNLPGTLVSSTTNQFTTSSQRAAVDAHYNLGKVYDYFYQKFNRNSYDNKGGKIVSSVHYGSRYNNAAWIGDQMIYGDGDGSFFSPLSGSMDVTAHEMTHGVTQETANLNYENQPGALNESFSDVFGYFNDTEDWDIGEDITVSQPALRSLSNPTKYGQPDNFKNYKNLPNTDAGDYGGVHTNSGIPNKAAYNTITKIGVNKAEQIYYRALTVYLTPSSTFKDAKAALIQSARDLYGSQDAASVEAAWNAVGL |
| Enzyme Length | 521 |
| Uniprot Accession Number | P06832 |
| Absorption | |
| Active Site | ACT_SITE 365; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 449; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Similar, but not identical, to that of thermolysin.; EC=3.4.24.28; |
| DNA Binding | |
| EC Number | 3.4.24.28 |
| Enzyme Function | FUNCTION: Extracellular zinc metalloprotease. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermolabile.; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (13); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 56,840 |
| Kinetics | |
| Metal Binding | METAL 283; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000255; METAL 360; /note=Calcium 2; /evidence=ECO:0000255; METAL 364; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 368; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 388; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 399; /note=Calcium 2; /evidence=ECO:0000255; METAL 399; /note=Calcium 3; /evidence=ECO:0000255; METAL 402; /note=Calcium 2; /evidence=ECO:0000255; METAL 402; /note=Calcium 3; /evidence=ECO:0000255; METAL 404; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000255; METAL 407; /note=Calcium 2; /evidence=ECO:0000255; METAL 407; /note=Calcium 3; /evidence=ECO:0000255; METAL 411; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000255 |
| Rhea ID | |
| Cross Reference Brenda |