| IED ID | IndEnz0002010192 |
| Enzyme Type ID | protease010192 |
| Protein Name |
Subtilisin-like protease 2 EC 3.4.21.- Destructin-1 Serine protease 2 PdSP2 |
| Gene Name | SP2 GMDG_06417 |
| Organism | Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat white-nose syndrome fungus) (Geomyces destructans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Leotiomycetes Leotiomycetes incertae sedis Pseudeurotiaceae Pseudogymnoascus Pseudogymnoascus destructans Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat white-nose syndrome fungus) (Geomyces destructans) |
| Enzyme Sequence | MKFSQSLIALAACFLPLIAAAPEEAQHAKIRSPGAQDIILDSYIVVFNKGVNDADIESEFASVSHILSKRRPAHKGVGHKYNITGFKGYQIETDTGSIGEIAASPLVAWIERDGKVQANALETRSGATWGLGRISHKATGSNSYVYDSSAGSGSTVYVVDSGIYIEHSEFEGRAKWGANYISGSPDTDENGHGTHCAGTIAGATYGVASKANLVAVKVLDGDGSGSNSGVIAGINFVGQNGKDGKSVLSMSLGGSYSAALNSAVESTISNGVTVVVAAGNDGADASNYSPASAKNAITVGAVDSTDTRADFSNYGSVLDVFAPGVDVKSAWIGSKSASNTISGTSMATPHVAGLAAYLIGLGGLSSPAAVASKIASIGIQGSVKDPKGSVNLIAYNGNGA |
| Enzyme Length | 400 |
| Uniprot Accession Number | L8FSM5 |
| Absorption | |
| Active Site | ACT_SITE 160; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 192; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 345; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | ACTIVITY REGULATION: Potently inhibited by the serine peptidase inhibitor chymostatin. Also inhibited by antpain and PMSF. {ECO:0000269|PubMed:25944934}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Major secreted subtilisin-like serine endopeptidase. Preferentially cleaves substrates containing hydrophobic residues at P4, positively charged residues at P3, small or flexible residues at P2, and large, bulky residues at P1. Mediates the degradation of collagen, the major structural protein in the mammalian host. Degrades the nonhelical regions of collagen that function in the cross-linking of the helical components (PubMed:25944934). May function as virulence factor involved in epidermal wing necrosis observed in white nose syndrome (WNS) in bats (By similarity). {ECO:0000250|UniProtKB:L8G6I7, ECO:0000269|PubMed:25944934}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 20-30 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9-10. {ECO:0000269|PubMed:25944934}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (2); Glycosylation (1); Propeptide (1); Signal peptide (1); Site (1) |
| Keywords | Direct protein sequencing;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25944934}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 40,489 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |