| IED ID | IndEnz0002009648 |
| Enzyme Type ID | protease009648 |
| Protein Name |
Serralysin EC 3.4.24.40 Protease PrtA Secreted alkaline metalloproteinase |
| Gene Name | prtA |
| Organism | Photorhabdus sp. (strain Az29) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Morganellaceae Photorhabdus unclassified Photorhabdus Photorhabdus sp. (strain Az29) |
| Enzyme Sequence | MERYMSLKKKISYSELIGSAKANELQTQLQAYVPGKDPNIVVEHEPSKNAAKELIRGDYRWGHQGDDKSETFQLTYSFLESEPDNMPWHITGFSAFNEEQRTAAKLSIQSWTDVANINFTETTDSDKAHITFGFFDASLTGSYAFAYLPSPESKQSGTWYNLKSRTFSENDIGVNGYGRQTFTHEIGHTLGLEHPAAYNASDKERPTYKKSATYFEDSRAYTVMSYFGEKNTRTDFKGIYSSAPLLNDISAIQEVYGANNTTRTDDTVYGFNSNTDRDFFTAKDENSKLLFTAWDAGGNDTFDFSGFTQDQRINLNEASFSDVGGLKGNVSIARGVTIENAIGGSGNDILIGNDAENILKGGAGDDIIYGGLGADQLWGGEGKDTFVYLSAKESPPLERDWIHDFVSGEDKIDVSLFDLGEAGKGGVKFVREFTGAVGEAVLRYDTVNKVNDFAINLGDKFSYDDFWVKIVGEPILESDFILA |
| Enzyme Length | 483 |
| Uniprot Accession Number | P82115 |
| Absorption | |
| Active Site | ACT_SITE 185; /evidence="ECO:0000250|UniProtKB:P07268, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by 8 mM 1,10-phenanthroline and 10 mM EDTA, but not by PMSF. {ECO:0000269|PubMed:15240252}. |
| 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: Involved in the inhibition of insect antibacterial peptides. Reduces the antibacterial activity of G.mellonella hemolymph by 50%. Reduces the antibacterial activity of cecropin A by 80% and cecropin B by 75%. {ECO:0000269|PubMed:15240252}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Active from 10 to 80 degrees Celsius. {ECO:0000269|PubMed:15240252}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:15240252}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (12); Repeat (2) |
| Keywords | Calcium;Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Repeat;Secreted;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15240252}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 53,483 |
| Kinetics | |
| Metal Binding | METAL 184; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:P07268, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 188; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:P07268, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 194; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:P07268, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 263; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:P07268"; METAL 266; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:P07268"; METAL 295; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:P07268"; METAL 297; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:P07268"; METAL 298; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:P07268"; METAL 300; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:P07268"; METAL 300; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:P07268"; METAL 337; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:P07268"; METAL 339; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:P07268" |
| Rhea ID | |
| Cross Reference Brenda |