| IED ID | IndEnz0001000386 |
| Enzyme Type ID | amylase000386 |
| Protein Name |
Bacillolysin EC 3.4.24.28 Neutral protease |
| Gene Name | npr |
| Organism | Paenibacillus polymyxa (Bacillus polymyxa) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Paenibacillaceae Paenibacillus Paenibacillus polymyxa (Bacillus polymyxa) |
| Enzyme Sequence | MKKVWFSLLGGAMLLGSVASGASAESSVSGPAQLTPTFHTEQWKAPSSVSGDDIVWSYLNRQKKSLLGVDSSSVREQFRIVDRTSDKSGVSHYRLKQYVNGIPVYGAEQTIHVGKSGEVTSYLGAVINEDQQEEATQGTTPKISASEAVYTAYKEAAARIEALPTSDDTISKDAEEPSSVSKDTYAEAANNDKTLSVDKDELSLDKASVLKDSKIEAVEAEKSSIAKIANLQPEVDPKAELYYYPKGDDLLLVYVTEVNVLEPAPLRTRYIIDANDGSIVFQYDIINEATGKGVLGDSKSFTTTASGSSYQLKDTTRGNGIVTYTASNRQSIPGTLLTDADNVWNDPAGVDAHAYAAKTYDYYKSKFGRNSIDGRGLQLRSTVHYGSRYNNAFWNGSQMTYGDGDGDGSTFIAFSGDPDVVGHELTHGVTEYTSNLEYYGESGALNEAFSDVIGNDIQRKNWLVGDDIYTPNICGDALRSMSNPTLYDQPHHYSNLYKGSSDNGGVHTNSGIINKAYYLLAQGGTFHGVTVNGIGRDAAVQIYYSAFTNYLTSSSDFSNARAAVIQAAKDLYGANSAEATAAAKSFDAVG |
| Enzyme Length | 590 |
| Uniprot Accession Number | P29148 |
| Absorption | |
| Active Site | ACT_SITE 424; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; ACT_SITE 507; /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: Involved in the generation of beta- and alpha-amylases from the large amylase precursor. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (14); Chain (1); Helix (11); Metal binding (12); Propeptide (1); Sequence conflict (1); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;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..24; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 4GER; |
| Mapped Pubmed ID | 23275160; |
| Motif | |
| Gene Encoded By | |
| Mass | 63,529 |
| Kinetics | |
| Metal Binding | METAL 339; /note=Calcium 1; /evidence=ECO:0000255; METAL 341; /note=Calcium 1; /evidence=ECO:0000255; METAL 419; /note=Calcium 2; /evidence=ECO:0000255; METAL 423; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 427; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 447; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 466; /note=Calcium 2; /evidence=ECO:0000255; METAL 466; /note=Calcium 3; /evidence=ECO:0000255; METAL 469; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000255; METAL 470; /note=Calcium 4; /evidence=ECO:0000255; METAL 473; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000255; METAL 476; /note=Calcium 4; /evidence=ECO:0000255 |
| Rhea ID | |
| Cross Reference Brenda |