| IED ID | IndEnz0002003777 |
| Enzyme Type ID | protease003777 |
| Protein Name |
Bacillolysin EC 3.4.24.28 Neutral protease |
| Gene Name | npr nprC |
| Organism | Bacillus cereus |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus cereus group Bacillus cereus |
| Enzyme Sequence | MKKKSLALVLATGMAVTTFGGTGSAFADSKNVLSTKKYNETVQSPEFISGDLTEATGKKAESVVFDYLNAAKGDYKLGEKSAQDSFKVKQVKKDAVTDSTVVRMQQVYEGVPVWGSTQVAHVSKDGSLKVLSGTVAPDLDKKEKLKNKNKIEGAKAIEIAQQDLGVTPKYEVEPKADLYVYQNGEETTYAYVVNLNFLDPSPGNYYYFIEADSGKVLNKFNTIDHVTNDDKSPVKQEAPKQDAKAVVKPVTGTNKVGTGKGVLGDTKSLNTTLSGSSYYLQDNTRGATIFTYDAKNRSTLPGTLWADADNVFNAAYDAAAVDAHYYAGKTYDYYKATFNRNSINDAGAPLKSTVHYGSNYNNAFWNGSQMVYGDGDGVTFTSLSGGIDVIGHELTHAVTENSSNLIYQNESGALNEAISDIFGTLVEFYDNRNPDWEIGEDIYTPGKAGDALRSMSDPTKYGDPDHYSKRYTGSSDNGGVHTNSGIINKQAYLLANGGTHYGVTVTGIGKDKLGAIYYRANTQYFTQSTTFSQARAGAVQAAADLYGANSAEVAAVKQSFSAVGVN |
| Enzyme Length | 566 |
| Uniprot Accession Number | P05806 |
| Absorption | |
| Active Site | ACT_SITE 393; ACT_SITE 481; /note=Proton donor |
| 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); Beta strand (15); Chain (1); Helix (11); Metal binding (19); Propeptide (1); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 1ESP; 1NPC; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 60,919 |
| Kinetics | |
| Metal Binding | METAL 307; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:15299677"; METAL 309; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:15299677"; METAL 311; /note="Calcium 1; via carbonyl oxygen"; METAL 388; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:15299677"; METAL 392; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:15299677"; METAL 396; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:15299677"; METAL 416; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:15299677"; METAL 427; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:15299677"; METAL 427; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:15299677"; METAL 433; /note="Calcium 3; via carbonyl oxygen"; METAL 435; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:15299677"; METAL 435; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:15299677"; METAL 437; /note="Calcium 2; via carbonyl oxygen"; METAL 440; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:15299677"; METAL 440; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:15299677"; METAL 443; /note="Calcium 4; via carbonyl oxygen"; METAL 444; /note="Calcium 4"; /evidence="ECO:0000269|PubMed:15299677"; METAL 447; /note="Calcium 4; via carbonyl oxygen"; METAL 450; /note="Calcium 4"; /evidence="ECO:0000269|PubMed:15299677" |
| Rhea ID | |
| Cross Reference Brenda |