| IED ID | IndEnz0002011746 |
| Enzyme Type ID | protease011746 |
| Protein Name |
Protease PrtS EC 3.4.24.- |
| Gene Name | prtS |
| Organism | Photorhabdus sp. (strain Az29) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Morganellaceae Photorhabdus unclassified Photorhabdus Photorhabdus sp. (strain Az29) |
| Enzyme Sequence | MQIQNNNYKGLIPPYILQNIYKNTSESEKDNVLMTLNHTQSLMLDSVIKTSDSIDNTDDEVVSDTLHRSIYDAKNETKLPGTLVRDEGDPDNGDVAVDNAYKYLEATYNFYKEVFNRNSLDDKGMKLIATVHYGKEYMNAYWGRGQMVFGDGDGKVFNNFTTSIDVIGHELSHGVIEKTADLIYFFQSGALNESIADVFGSLVRQHYLKQKADEASWVVGEELLAKGIKGVGIRSMKEPGKAYDDPLLGKNPQPGHMDDFKDYPIYRDNGGVHVNSGIPNKAFYNLAIKLGGYAWEKAGKIWYNTLLDKDLARDTTFLSFAKLTVKHARDLFDEDVEKATIDSWKEVGIKVKEEDKDKGKDEGKDKAETKV |
| Enzyme Length | 371 |
| Uniprot Accession Number | A9YWT8 |
| Absorption | |
| Active Site | ACT_SITE 170; /evidence="ECO:0000250|UniProtKB:P05806, ECO:0000255|PROSITE-ProRule:PRU10095"; ACT_SITE 273; /note="Proton donor"; /evidence="ECO:0000250|UniProtKB:P05806, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by 8 mM 1,10-phenanthroline, but not by EDTA or PMSF. {ECO:0000269|PubMed:15240252}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Metalloprotease 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 completely inhibits cecropin B. {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 7.0. {ECO:0000269|PubMed:15240252}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (3); Region (1); Sequence conflict (2); Signal peptide (1) |
| Keywords | Direct protein sequencing;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15240252}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..?; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,773 |
| Kinetics | |
| Metal Binding | METAL 169; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:P05806, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 173; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:P05806, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 193; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:P05806, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Rhea ID | |
| Cross Reference Brenda |