| IED ID | IndEnz0002015656 |
| Enzyme Type ID | protease015656 |
| Protein Name |
Bacillolysin EC 3.4.24.28 Neutral protease |
| Gene Name | nprM BMD_2285 |
| Organism | Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Priestia Priestia megaterium (Bacillus megaterium) Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium) |
| Enzyme Sequence | MKKKKQALKVLLSVGILSSSFAFAHTSSAAPNNVLSTEKYNKEIKSPEFISGKLSGPSSQKAQDVVFHYMNTNKDKYKLGNENAQNSFKVTEVVKDPVEQATVVRLQQVYNNIPVWGSTQLAHVAKDGTLKVVSGTVAPDLDKKEKLKGQKQVDSKKAIQAAEKDLGFKPTYEKSPSSELYVYQNGSDTTYAYVVNLNFLSPEPGNYYYFVDAISGKVLDKYNTIDSVAGPKADVKQAAKPAAKPVTGTNAIGSGKGVLGDTKSLKTTLSSSTYYLQDNTRGATIYTYDAKNRTSLPGTLWTDTDNTYNATRDAAAVDAHYYAGVTYDYYKNKFNRNSYDNAGAPLKSTVHYSSGYNNAFWNGSQMVYGDGDGTTFVPLSGGLDVIGHELTHAVTERSSNLIYQYESGALNEAISDIFGTLVEYYDNRNPDWEIGEDIYTPGTSGDALRSMSNPAKYGDPDHYSKRYTGSSDNGGVHTNSGIINKAAYLLANGGTHYGVTVTGIGGDKLGKIYYRANTLYFTQSTTFSQARAGLVQAAADLYGSGSQEVISVGKSFDAVGVQ |
| Enzyme Length | 562 |
| Uniprot Accession Number | D5DEH5 |
| Absorption | |
| Active Site | ACT_SITE 389; /evidence=ECO:0000250|UniProtKB:P05806; ACT_SITE 477; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P05806 |
| 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. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (17); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 60,862 |
| Kinetics | |
| Metal Binding | METAL 303; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P05806; METAL 305; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P05806; METAL 384; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P05806; METAL 388; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P05806; METAL 392; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P05806; METAL 412; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:P05806; METAL 423; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P05806; METAL 423; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P05806; METAL 429; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P05806; METAL 431; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P05806; METAL 431; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P05806; METAL 433; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P05806; METAL 436; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P05806; METAL 436; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P05806; METAL 439; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P05806; METAL 440; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:P05806; METAL 446; /note=Calcium 4; /evidence=ECO:0000250|UniProtKB:P05806 |
| Rhea ID | |
| Cross Reference Brenda |