| IED ID | IndEnz0002009471 |
| Enzyme Type ID | protease009471 |
| 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 ERDMAN_3146 |
| Organism | Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman) |
| Enzyme Sequence | MMFVTGIVLFALAILISVALHECGHMWVARRTGMKVRRYFVGFGPTLWSTRRGETEYGVKAVPLGGFCDIAGMTPVEELDPDERDRAMYKQATWKRVAVLFAGPGMNLAICLVLIYAIALVWGLPNLHPPTRAVIGETGCVAQEVSQGKLEQCTGPGPAALAGIRSGDVVVKVGDTPVSSFDEMAAAVRKSHGSVPIVVERDGTAIVTYVDIESTQRWIPNGQGGELQPATVGAIGVGAARVGPVRYGVFSAMPATFAVTGDLTVEVGKALAALPTKVGALVRAIGGGQRDPQTPISVVGASIIGGDTVDHGLWVAFWFFLAQLNLILAAINLLPLLPFDGGHIAVAVFERIRNMVRSARGKVAAAPVNYLKLLPATYVVLVLVVGYMLLTVTADLVNPIRLFQ |
| Enzyme Length | 404 |
| Uniprot Accession Number | H8EW46 |
| 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 site-2 protease (S2P) that cleaves type-2 transmembrane proteins within their membrane-spanning domains. Degrades anti-sigma factors RskA, RslA and RsmA, releasing sigma factors SigK, SigL and SigM from the cellular membrane, activating signaling pathways. Does not act on RsdA. Regulates the composition of extractable mycolic acids in the cell envelope in response to changes in membrane fluidity. Mediates transcriptional regulation of mycolic acid biosynthetic genes in response to detergent. Probably also cleaves PbpB (PBP3, FtsI); this cleavage is inhibited by Wag31-PbpBI interaction. {ECO:0000269|PubMed:20545848}.; 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) 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). {ECO:0000269|PubMed:20545848}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Metal binding (3); Mutagenesis (1); Transmembrane (4) |
| Keywords | Cell membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Transmembrane;Transmembrane helix;Virulence;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 | 42,834 |
| 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 |