| IED ID | IndEnz0002015657 |
| Enzyme Type ID | protease015657 |
| Protein Name |
Thermostable neutral protease NprT Thermostable neutral proteinase EC 3.4.24.- Stearolysin Thermolysin-like protease |
| Gene Name | nprT |
| Organism | Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Geobacillus Geobacillus stearothermophilus (Bacillus stearothermophilus) |
| Enzyme Sequence | MNKRAMLGAIGLAFGLLAAPIGASAKGESIVWNEQWKTPSFVSGSLLNGGEQALEELVYQYVDRENGTFRLGGRARDRLALIGKQTDELGHTVMRFEQRHHGIPVYGTMLAAHVKDGELIALSGSLIPNLDGQPRLKKAKTVTVQQAEAIAEQDVTETVTKERPTTENGERTRLVIYPTDGTARLAYEVNVRFLTPVPGNWVYIIDATDGAILNKFNQIDSRQPGGGQPVAGASTVGVGRGVLGDQKYINTTYSSYYGYYYLQDNTRGSGIFTYDGRNRTVLPGSLWTDGDNQFTASYDAAAVDAHYYAGVVYDYYKNVHGRLSYDGSNAAIRSTVHYGRGYNNAFWNGSQMVYGDGDGQTFLPFSGGIDVVGHELTHAVTDYTAGLVYQNESGAINEAMSDIFGTLVEFYANRNPDWEIGEDIYTPGVAGDALRSMSDPAKYGDPDHYSKRYTGTQDNGGVHTNSGIINKAAYLLSQGGVHYGVSVNGIGRDKMGKIFYRALVYYLTPTSNFSQLRAACVQAAADLYGSTSQEVNSVKQAFNAVGVY |
| Enzyme Length | 548 |
| Uniprot Accession Number | P06874 |
| Absorption | |
| Active Site | ACT_SITE 375; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 463; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Its casein hydrolytic activity is inhibited almost completely by a chelating agent (EDTA), whereas neither diisopropyl fluorophosphate nor phenylmethylsulfonyl fluoride inhibit the proteolytic activity in vitro. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Extracellular zinc metalloprotease. {ECO:0000269|PubMed:6302083}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. Retains about 80% of its activity after treatment of 65 degrees Celsius for 30 minutes. {ECO:0000269|PubMed:6302083}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 7. {ECO:0000269|PubMed:6302083}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (19); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6302083}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 59,580 |
| Kinetics | |
| Metal Binding | METAL 289; /note=Calcium 1; /evidence=ECO:0000250; METAL 291; /note=Calcium 1; /evidence=ECO:0000250; METAL 293; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 370; /note=Calcium 2; /evidence=ECO:0000250; METAL 374; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 378; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 398; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 409; /note=Calcium 2; /evidence=ECO:0000250; METAL 409; /note=Calcium 3; /evidence=ECO:0000250; METAL 415; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 417; /note=Calcium 2; /evidence=ECO:0000250; METAL 417; /note=Calcium 3; /evidence=ECO:0000250; METAL 419; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 422; /note=Calcium 2; /evidence=ECO:0000250; METAL 422; /note=Calcium 3; /evidence=ECO:0000250; METAL 425; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 426; /note=Calcium 4; /evidence=ECO:0000250; METAL 429; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 432; /note=Calcium 4; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |