| IED ID | IndEnz0002009017 |
| Enzyme Type ID | protease009017 |
| Protein Name |
Streptopain EC 3.4.22.10 Exotoxin type B SPE B Streptococcal cysteine proteinase Streptococcus peptidase A SPP |
| Gene Name | speB SPy_2039 M5005_Spy1735 |
| Organism | Streptococcus pyogenes serotype M1 |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus pyogenes Streptococcus pyogenes serotype M1 |
| Enzyme Sequence | MNKKKLGVRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRGDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP |
| Enzyme Length | 398 |
| Uniprot Accession Number | P0C0J1 |
| Absorption | |
| Active Site | ACT_SITE 192; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 340; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage with hydrophobic residues at P2, P1 and P1'.; EC=3.4.22.10; Evidence={ECO:0000269|PubMed:19237546}; |
| DNA Binding | |
| EC Number | 3.4.22.10 |
| Enzyme Function | FUNCTION: Important streptococcal virulence factor which cleaves human fibronectin and degrades vitronectin. Also cleaves human IL1B precursor to form biologically active IL1B. Can induce apoptosis in human monocytes and epithelial cells in vitro, and reduces phagocytic activity in monocytic cells. Thus, may play a role in bacterial colonization, invasion, and inhibition of wound healing. {ECO:0000269|PubMed:10456871}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (11); Chain (1); Helix (8); Modified residue (1); Mutagenesis (4); Natural variant (3); Propeptide (1); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Hydrolase;Methylation;Protease;Reference proteome;Secreted;Signal;Thiol protease;Toxin;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 192; /note=Cysteine methyl disulfide; in zymogen form; /evidence=ECO:0000250 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000250 |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 2JTC; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,130 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |