| IED ID | IndEnz0002012236 |
| Enzyme Type ID | protease012236 |
| Protein Name |
Thermolysin EC 3.4.24.27 Neutral protease |
| Gene Name | nprS nprM |
| Organism | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Geobacillus Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Enzyme Sequence | MKRKMKMKLVRFGLAAGLAAQVFFLPYNALASTEHVTWNQQFQTPQFISGDLLKVNGTSPEELVYQYVEKNENKFKFHENAKDTLQLKEKKNDNLGFTFMRFQQTYKGIPVFGAVVTAHVKDGTLTALSGTLIPNLDTKGSLKSGKKLSEKQARDIAEKDLVANVTKEVPEYEQGKDTEFVVYVNGDEASLAYVVNLNFLTPEPGNWLYIIDAVDGKILNKFNQLDAAKPGDVKSITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK |
| Enzyme Length | 551 |
| Uniprot Accession Number | P43133 |
| Absorption | |
| Active Site | ACT_SITE 378; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 466; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.; EC=3.4.24.27; |
| DNA Binding | |
| EC Number | 3.4.24.27 |
| Enzyme Function | FUNCTION: Extracellular zinc metalloprotease. {ECO:0000269|PubMed:3149972}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. Retains about 45% of its activity after treatment of 90 degrees Celsius for 30 minutes. {ECO:0000269|PubMed:3149972}; |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (14); Chain (1); Helix (12); Metal binding (18); Propeptide (1); Sequence conflict (8); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | INDUCTION: Is expressed in the stationary phase. Up-regulated by NprA. {ECO:0000269|PubMed:2203733}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3149972}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (15) |
| Cross Reference PDB | 5DLH; 5ONP; 5ONQ; 5WR2; 5WR3; 5WR4; 5WR5; 5WR6; 6FHP; 6FSM; 6GHX; 6Y4I; 6YI6; 6YMR; 6YMS; |
| Mapped Pubmed ID | 28777085; 29717999; 30171661; 30403288; |
| Motif | |
| Gene Encoded By | |
| Mass | 60,617 |
| Kinetics | |
| Metal Binding | METAL 292; /note=Calcium 1; /evidence=ECO:0000250; METAL 294; /note=Calcium 1; /evidence=ECO:0000250; METAL 296; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 373; /note=Calcium 2; /evidence=ECO:0000250; METAL 377; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 381; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 401; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 412; /note=Calcium 2; /evidence=ECO:0000250; METAL 412; /note=Calcium 3; /evidence=ECO:0000250; METAL 418; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 420; /note=Calcium 2; /evidence=ECO:0000250; METAL 420; /note=Calcium 3; /evidence=ECO:0000250; METAL 422; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 425; /note=Calcium 2; /evidence=ECO:0000250; METAL 425; /note=Calcium 3; /evidence=ECO:0000250; METAL 429; /note=Calcium 4; /evidence=ECO:0000250; METAL 432; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 435; /note=Calcium 4; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.28; |