Detail Information for IndEnz0002010012
IED ID IndEnz0002010012
Enzyme Type ID protease010012
Protein Name Zinc metalloprotease Rip1
EC 3.4.24.-
S2P endopeptidase
Site-2 protease Rip1
S2P protease Rip1
Site-2-type intramembrane protease
Gene Name rip1 ML1582
Organism Mycobacterium leprae (strain TN)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium leprae Mycobacterium leprae (strain TN)
Enzyme Sequence MMFALGIVLFAIAILISVALHECGHLWVACATGMKVRRYFVGFGPTLWSTRRGETQYGIKAVPLGGFCDIVGMTSVEKLEPDESDRAMYKQATWKRVAVLFAGPAMNFVICLVLIYGIALVWGLPNLHMPTRAVIGETACVASELDQGKLGNCTGPGPAALAGLRAGDVVVKIGDTTVSTFDDMAAVVRKLHGTVPIVFERDGTAITSYVDITPTQRYMSKGKGSQLEPATVGAIGVGAHHLLPTHYGVFSALPATAAFAGDLTVEVGKALVTIPTKLGALVHAIGGGQRDPQTPMSVVGASIIGGDTVDHGLWVAFWFFLAQLNLILGAINLVPLLPFDGGHIAIAVFERIRNLIRSARGVVVAAPVNYLKLMPATYVVLVFVVGYVLLTVTADLVNPIRLFQ
Enzyme Length 404
Uniprot Accession Number Q9CBU4
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. 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 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. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Domain (1); Metal binding (2); Transmembrane (4)
Keywords Cell membrane;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;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 42,875
Kinetics
Metal Binding METAL 21; /note=Zinc; catalytic; /evidence=ECO:0000255; METAL 25; /note=Zinc; catalytic; /evidence=ECO:0000255
Rhea ID
Cross Reference Brenda