| IED ID | IndEnz0002009893 |
| Enzyme Type ID | protease009893 |
| Protein Name |
Zinc metalloprotease Rip1 EC 3.4.24.- Regulator of sigma KLM proteases S2P endopeptidase Site-2-type intramembrane protease site-2 protease Rip1 S2P protease Rip1 |
| Gene Name | rip1 BCG_2891c |
| Organism | Mycobacterium bovis (strain BCG / Pasteur 1173P2) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium bovis Mycobacterium tuberculosis variant bovis BCG Mycobacterium bovis (strain BCG / Pasteur 1173P2) |
| Enzyme Sequence | MMFVTGIVLFALAILISVALHECGHMWVARRTGMKVRRYFVGFGPTLWSTRRGETEYGVKAVPLGGFCDIAGMTPVEELDPDERDRAMYKQATWKRVAVLFAGPGMNLAICLVLIYAIALVWGLPNLHPPTRAVIGETGCVAQEVSQGKLEQCTGPGPAALAGIRSGDVVVKVGDTPVSSFDEMAAAVRKSHGSVPIVVERDGTAIVTYVDIESTQRWIPNGQGGELQPATVGAIGVGAARVGPVRYGVFSAMPATFAFTGDLTVEVGKALAALPTKVGALVRAIGGGQRDPQTPISVVGASIIGGDTVDHGLWVAFWFFLAQLNLILATINLLPLLPFDGGHIAVAVFERIRNMVRSARGKVAAAPVNYLKLLPATYVVLVLVVGYMLLTVTADLVNPIRLFQ |
| Enzyme Length | 404 |
| Uniprot Accession Number | A1KML4 |
| Absorption | |
| Active Site | ACT_SITE 22; /evidence=ECO:0000255 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: A probable intramembrane site-2 protease (S2P) that cleaves type-2 transmembrane proteins within their membrane-spanning domains. Cleaves PbpB (PBP3, FtsI); cleavage is inhibited by Wag31-PbpB interaction. Probably also cleaves anti-sigma factors RskA, RslA and RsmA. {ECO:0000250}.; FUNCTION: Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal (possibly oxidative stress) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein (includes anti-sigma factors RskA, RslA, RsmA, and PbpB in M.tuberculosis) is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this entry), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein (ECF sigma factors SigK, SigL and SigM) (Probable). {ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Metal binding (3); Mutagenesis (2); Transmembrane (4) |
| Keywords | Cell membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,912 |
| Kinetics | |
| Metal Binding | METAL 21; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 25; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 202; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |