| IED ID | IndEnz0002011263 |
| Enzyme Type ID | protease011263 |
| Protein Name |
Thermolysin EC 3.4.24.27 Thermostable neutral proteinase |
| Gene Name | |
| Organism | Alicyclobacillus acidocaldarius subsp. acidocaldarius (Bacillus acidocaldarius) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Alicyclobacillaceae Alicyclobacillus Alicyclobacillus acidocaldarius Alicyclobacillus acidocaldarius subsp. acidocaldarius (Bacillus acidocaldarius) |
| Enzyme Sequence | MNKRAMLGAIGLAFGLMAWPFGASAKEKSMVWNEQWKTPSFVSGSLLKGEDAPEELVYRYLDQEKNTFQLGGQARERLSLIGKQTDELGHTVMRFEQRYRGIPVYGAVLVAHVNDGELSSLSGTLIPNLDKRTLKTEAAISIQQAEMIAKQDVADAVTKERPAAEEGKPTRLVIYPDGETPRLAYEVNVRFLTPVPGNWIYMIDAADGKVLNKWNQMDEAKPGGGQPVAGTSTVGVGRGVLGDQKYINTTYSSYYGYYYLQDNTRGSGIFTYDGRNRTVLPGSLWADGDNQFFASYDAAAVDAHYYAGVVYDYYKNVHGRLSYDGSNAAIRSTVHYGRGYNNAFWNGSQMVYGDGDGQTFLPFSGGIDVVGHELTHAVTDYTAGLVYQNESGAINEAMSDIFGTLVEFYANRNPDWEIGEDIYTPGIAGDALRSMSDPAKYGDPDHYSKRYTGTQDNGGVHTNSGIINKAAYLLSQGGVHYGVSVTGIGRDKMGKIFYRALVYYLTPTSNFSQLRAACVQAAADLYGSTSQEVNSVKQAFNAVGVY |
| Enzyme Length | 546 |
| Uniprot Accession Number | Q43880 |
| Absorption | |
| Active Site | ACT_SITE 373; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 461; /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. |
| 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; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 59,770 |
| Kinetics | |
| Metal Binding | METAL 287; /note=Calcium 1; /evidence=ECO:0000250; METAL 289; /note=Calcium 1; /evidence=ECO:0000250; METAL 291; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 368; /note=Calcium 2; /evidence=ECO:0000250; METAL 372; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 376; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 396; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 407; /note=Calcium 2; /evidence=ECO:0000250; METAL 407; /note=Calcium 3; /evidence=ECO:0000250; METAL 413; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 415; /note=Calcium 2; /evidence=ECO:0000250; METAL 415; /note=Calcium 3; /evidence=ECO:0000250; METAL 417; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 420; /note=Calcium 2; /evidence=ECO:0000250; METAL 420; /note=Calcium 3; /evidence=ECO:0000250; METAL 423; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 424; /note=Calcium 4; /evidence=ECO:0000250; METAL 427; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 430; /note=Calcium 4; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |