| IED ID | IndEnz0002015654 |
| Enzyme Type ID | protease015654 |
| Protein Name |
Neutral protease B EC 3.4.24.- |
| Gene Name | nprB BSU11100 |
| Organism | Bacillus subtilis (strain 168) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Bacillaceae Bacillus Bacillus subtilis group Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis (strain 168) |
| Enzyme Sequence | MRNLTKTSLLLAGLCTAAQMVFVTHASAEESIEYDHTYQTPSYIIEKSPQKPVQNTTQKESLFSYLDKHQTQFKLKGNANSHFRVSKTIKDPKTKQTFFKLTEVYKGIPIYGFEQAVAMKENKQVKSFFGKVHPQIKDVSVTPSISEKKAIHTARRELEASIGKIEYLDGEPKGELYIYPHDGEYDLAYLVRLSTSEPEPGYWHYFIDAKNGKVIESFNAIHEAAGTGIGVSGDEKSFDVTEQNGRFYLADETRGKGINTFDAKNLNETLFTLLSQLIGYTGKEIVSGTSVFNEPAAVDAHANAQAVYDYYSKTFGRDSFDQNGARITSTVHVGKQWNNAAWNGVQMVYGDGDGSKFKPLSGSLDIVAHEITHAVTQYSAGLLYQGEPGALNESISDIMGAMADRDDWEIGEDVYTPGIAGDSLRSLEDPSKQGNPDHYSNRYTGTEDYGGVHINSSIHNKAAYLLAEGGVHHGVQVEGIGREASEQIYYRALTYYVTASTDFSMMKQAAIEAANDLYGEGSKQSASVEKAYEAVGIL |
| Enzyme Length | 538 |
| Uniprot Accession Number | P39899 |
| Absorption | |
| Active Site | ACT_SITE 370; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 453; /note=Proton donor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Protease activity can be inhibited in vitro by either a zinc specific chelator, 1,10-phenanthroline, or a metal chelator, EDTA. The enzyme is resistant to phenylmethylsulfonyl fluoride and iodoacetic acid. {ECO:0000269|PubMed:1917867}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Protease able to cleave casein in vitro. {ECO:0000269|PubMed:1917867}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Retains 65% activity after treatment at 65 degrees Celsius for 20 minutes. {ECO:0000269|PubMed:1917867}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.6. {ECO:0000269|PubMed:1917867}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (16); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1917867}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..28; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 59,336 |
| Kinetics | |
| Metal Binding | METAL 365; /note="Calcium 1"; /evidence="ECO:0000255"; METAL 369; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:1917867"; METAL 373; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:1917867"; METAL 393; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:1917867"; METAL 404; /note="Calcium 1"; /evidence="ECO:0000255"; METAL 404; /note="Calcium 2"; /evidence="ECO:0000255"; METAL 406; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000255"; METAL 407; /note="Calcium 1"; /evidence="ECO:0000255"; METAL 407; /note="Calcium 2"; /evidence="ECO:0000255"; METAL 409; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000255"; METAL 412; /note="Calcium 1"; /evidence="ECO:0000255"; METAL 412; /note="Calcium 2"; /evidence="ECO:0000255"; METAL 415; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000255"; METAL 416; /note="Calcium 3"; /evidence="ECO:0000255"; METAL 419; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000255"; METAL 422; /note="Calcium 3"; /evidence="ECO:0000255" |
| Rhea ID | |
| Cross Reference Brenda |