IED ID | IndEnz0002008919 |
Enzyme Type ID | protease008919 |
Protein Name |
Protease RseP EC 3.4.24.- S2P endopeptidase Site-2 protease RseP S2P protease RseP Site-2-type intramembrane protease Fragment |
Gene Name | rseP |
Organism | Photorhabdus luminescens (Xenorhabdus luminescens) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Morganellaceae Photorhabdus Photorhabdus luminescens (Xenorhabdus luminescens) |
Enzyme Sequence | VEKVIPGSAAEKAGLQKGDRIVKVGSQEIDVWHTFTSFVSNNPNVPLELSVDRAGHIISLSMTPEVRQQSGGRKVGFAGVELRIVPLADEYKIVQQYGPFSAMYQAGDKTWQLMRLTVSMIGKLIVGDVKINNLSGPISIAKGAGVSADSGLVYYLMFLALISVNLGIINLIPLPVLDGGHLLFLFIEKIKGGPVSERVQDFSYRIGAMILVLLMGLALFNDFSRF |
Enzyme Length | 226 |
Uniprot Accession Number | Q9S342 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Domain (1); Non-terminal residue (1); Transmembrane (2) |
Keywords | Cell inner membrane;Cell membrane;Hydrolase;Membrane;Metalloprotease;Protease;Transmembrane;Transmembrane helix;Zinc |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 24,535 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |