| IED ID | IndEnz0002008893 | 
| Enzyme Type ID | protease008893 | 
| Protein Name | 
                        
                            
                                Serralysin  EC 3.4.24.40 Extracellular metalloproteinase Serratiopeptidase Serrapeptase Serrapeptidase Zinc proteinase  | 
                    
| Gene Name | |
| Organism | Serratia marcescens (strain ATCC 21074 / E-15) | 
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Yersiniaceae Serratia unclassified Serratia Serratia marcescens (strain ATCC 21074 / E-15) | 
| Enzyme Sequence | MQSTKKAIEITESNFAAATTGYDAVDDLLHYHERGNGIQINGKDSFSNEQAGLFITRENQTWNGYKVFGQPVKLTFSFPDYKFSSTNVAGDTGLSKFSAEQQQQAKLSLQSWADVANITFTEVAAGQKANITFGNYSQDRPGHYDYGTQAYAFLPNTIWQGQDLGGQTWYNVNQSNVKHPATEDYGRQTFTHEIGHALGLSHPGDYNAGEGNPTYRDVTYAEDTRQFSLMSYWSETNTGGDNGGHYAAAPLLDDIAAIQHLYGANLSTRTGDTVYGFNSNTGRDFLSTTSNSQKVIFAAWDAGGNDTFDFSGYTANQRINLNEKSFSDVGGLKGNVSIAAGVTIENAIGGSGNDVIVGNAANNVLKGGAGNDVLFGGGGADELWGGAGKDIFVFSAASDSAPGASDWIRDFQKGIDKIDLSFFNKEAQSSDFIHFVDHFSGAAGEALLSYNASNNVTDLSVNIGGHQAPDFLVKIVGQVDVATDFIV | 
| Enzyme Length | 487 | 
| Uniprot Accession Number | P07268 | 
| Absorption | |
| Active Site | ACT_SITE 193 | 
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of bonds with hydrophobic residues in P1'.; EC=3.4.24.40; | 
| DNA Binding | |
| EC Number | 3.4.24.40 | 
| Enzyme Function | FUNCTION: Naturally present in the silkworm intestine and allows the emerging moth to dissolve its cocoon. | 
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (28); Chain (1); Frameshift (1); Helix (11); Metal binding (40); Propeptide (1); Repeat (2); Turn (8) | 
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Repeat;Secreted;Zinc;Zymogen | 
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. | 
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) | 
| Cross Reference PDB | 1SRP; | 
| Mapped Pubmed ID | - | 
| Motif | |
| Gene Encoded By | |
| Mass | 52,235 | 
| Kinetics | |
| Metal Binding | METAL 192; /note=Zinc; catalytic; METAL 196; /note=Zinc; catalytic; METAL 202; /note=Zinc; catalytic; METAL 232; /note=Zinc; catalytic; METAL 269; /note=Calcium 1; via carbonyl oxygen; METAL 271; /note=Calcium 1; via carbonyl oxygen; METAL 273; /note=Calcium 1; METAL 301; /note=Calcium 1; METAL 303; /note=Calcium 1; via carbonyl oxygen; METAL 304; /note=Calcium 2; via carbonyl oxygen; METAL 306; /note=Calcium 1; METAL 306; /note=Calcium 2; METAL 343; /note=Calcium 2; via carbonyl oxygen; METAL 345; /note=Calcium 2; METAL 350; /note=Calcium 3; via carbonyl oxygen; METAL 352; /note=Calcium 3; via carbonyl oxygen; METAL 354; /note=Calcium 3; METAL 359; /note=Calcium 4; via carbonyl oxygen; METAL 361; /note=Calcium 4; via carbonyl oxygen; METAL 363; /note=Calcium 4; METAL 367; /note=Calcium 3; via carbonyl oxygen; METAL 368; /note=Calcium 5; via carbonyl oxygen; METAL 369; /note=Calcium 3; via carbonyl oxygen; METAL 372; /note=Calcium 3; METAL 372; /note=Calcium 5; METAL 376; /note=Calcium 4; via carbonyl oxygen; METAL 377; /note=Calcium 6; via carbonyl oxygen; METAL 378; /note=Calcium 4; via carbonyl oxygen; METAL 379; /note=Calcium 6; via carbonyl oxygen; METAL 381; /note=Calcium 4; METAL 381; /note=Calcium 6; METAL 385; /note=Calcium 5; via carbonyl oxygen; METAL 386; /note=Calcium 7; via carbonyl oxygen; METAL 387; /note=Calcium 5; via carbonyl oxygen; METAL 388; /note=Calcium 7; via carbonyl oxygen; METAL 390; /note=Calcium 5; METAL 390; /note=Calcium 7; METAL 399; /note=Calcium 6; METAL 406; /note=Calcium 6; METAL 416; /note=Calcium 7 | 
| Rhea ID | |
| Cross Reference Brenda |