| IED ID | IndEnz0002008036 |
| Enzyme Type ID | protease008036 |
| Protein Name |
Pro-Pro endopeptidase PPEP-2 EC 3.4.24.89 |
| Gene Name | PAV_1c07830 |
| Organism | Paenibacillus alvei (strain ATCC 6344 / DSM 29 / NBRC 3343 / NCIMB 9371 / NCTC 6352) (Bacillus alvei) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Bacilli Bacillales Paenibacillaceae Paenibacillus Paenibacillus alvei (Bacillus alvei) Paenibacillus alvei (strain ATCC 6344 / DSM 29 / NBRC 3343 / NCIMB 9371 / NCTC 6352) (Bacillus alvei) |
| Enzyme Sequence | MKWDKRVVALILAVMIVCPLFAAPAHAQEQSILDKLVVLPSGEYNHSEAAAMKQRLEKIPTSILDALYSKGVKIKLTQGAITNEPELAYLKGVVPRGWEGTGLTWDDVPGVSERVVAVRIGYSEKGKGHNSLNLEIHETLHAVDRLVLNEVSGTDEFINIFNKEASVKYKGDGYVSAYPTEYFAEAASLYLYSDATRSDLKDSMPLTYEFMAKLFAN |
| Enzyme Length | 217 |
| Uniprot Accession Number | K4ZRC1 |
| Absorption | |
| Active Site | ACT_SITE 138; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q183R7 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=The enzyme catalyzes the hydrolytic cleavage of peptide bonds between two proline residues.; EC=3.4.24.89; Evidence={ECO:0000269|PubMed:29794027}; |
| DNA Binding | |
| EC Number | 3.4.24.89 |
| Enzyme Function | FUNCTION: Zinc-dependent endoprotease with a unique preference for proline residues surrounding the scissile bond, which cleaves in a PLP-|-PVP motif. Cleaves the cell surface protein encoded by an adjacent gene, which contains two PPEP-2 cleaving sites and putative extracellular matrix-binding domains. Thereby, may have a role in the regulation of P.alvei adhesion. Is not able to cleave within the PVP-|-PVQ motif, and only shows a very poor cleavage of the VNP-|-PVP motif in vitro, which is the optimal substrate peptide for PPEP-1 from P.difficile. {ECO:0000269|PubMed:29794027}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (4); Chain (1); Helix (13); Metal binding (4); Mutagenesis (1); Region (1); Signal peptide (1); Site (1); Turn (2) |
| Keywords | 3D-structure;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29794027}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence="ECO:0000255, ECO:0000305|PubMed:29794027" |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 6FPC; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 24,015 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=70 uM for a FRET peptide containing PLPPVP {ECO:0000269|PubMed:29794027}; KM=330 uM for a FRET peptide containing VLPPVP {ECO:0000269|PubMed:29794027}; Note=kcat is 8 sec(-1) with a FRET peptide containing PLPPVP as substrate. kcat is 3 sec(-1) with a FRET peptide containing VLPPVP as substrate. {ECO:0000269|PubMed:29794027}; |
| Metal Binding | METAL 137; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:29794027; METAL 141; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:29794027; METAL 174; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:29794027; METAL 181; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:29794027 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.89; |