IED ID | IndEnz0002001124 |
Enzyme Type ID | protease001124 |
Protein Name |
Bacillolysin EC 3.4.24.28 Thermostable neutral protease |
Gene Name | npr |
Organism | Bacillus caldolyticus |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Geobacillus Geobacillus thermoleovorans group Bacillus caldolyticus |
Enzyme Sequence | MNKRAMLGAIGLAFGLMAWPFGASAKGKSMVWNEQWKTPSFVSGSLLGRCSQELVYRYLDQEKNTFQLGGQARERLSLIGNKLDELGHTVMRFEQAIAASLCMGAVLVAHVNDGELSSLSGTLIPNLDKRTLKTEAAISIQQAEMIAKQDVADRVTKERPAAEEGKPTRLVIYPDEETPRLAYEVNVRFLTPVPGNWIYMIDAADGKVLNKWNQMDEAKPGGAQPVAGTSTVGVGRGVLGDQKYINTTYSSYYGYYYLQDNTRGSGIFTYDGRNRTVLPGSLWADGDNQFFASYDAAAVDAHYYAGVVYDYYKNVHGRLSYDGSNAAIRSTVHYGRGYNNAFWNGSQMVYGDGDGQTFLPFSGGIDVVGHELTHAVTDYTAGLVYQNESGAINEAMSDIFGTLVEFYANRNPDWEIGEDIYTPGVAGDALRSMSDPAKYGDPDHYSKRYTGTQDNGGVHTNSGIINKAAYLLSQGGVHYGVSVTGIGRDKMGKIFYRALVYYLTPTSNFSQLRAACVQAAADLYGSTSQEVNSVKQAFNAVGVY |
Enzyme Length | 544 |
Uniprot Accession Number | P23384 |
Absorption | |
Active Site | ACT_SITE 371; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 459; /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: Thermostable.; |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Metal binding (19); 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..25 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 59,413 |
Kinetics | |
Metal Binding | METAL 285; /note=Calcium 1; /evidence=ECO:0000250; METAL 287; /note=Calcium 1; /evidence=ECO:0000250; METAL 289; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 366; /note=Calcium 2; /evidence=ECO:0000250; METAL 370; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 374; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 394; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 405; /note=Calcium 2; /evidence=ECO:0000250; METAL 405; /note=Calcium 3; /evidence=ECO:0000250; METAL 411; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 413; /note=Calcium 2; /evidence=ECO:0000250; METAL 413; /note=Calcium 3; /evidence=ECO:0000250; METAL 415; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 418; /note=Calcium 2; /evidence=ECO:0000250; METAL 418; /note=Calcium 3; /evidence=ECO:0000250; METAL 421; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 422; /note=Calcium 4; /evidence=ECO:0000250; METAL 425; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 428; /note=Calcium 4; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |