Detail Information for IndEnz0002008979
IED ID IndEnz0002008979
Enzyme Type ID protease008979
Protein Name Anti-sigma-L factor RslA
Regulator of SigL
Sigma-L anti-sigma factor RslA
Gene Name rslA MT0760
Organism Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
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 CDC 1551 / Oshkosh)
Enzyme Sequence MTMPLRGLGPPDDTGVREVSTGDDHHYAMWDAAYVLGALSAADRREFEAHLAGCPECRGAVTELCGVPALLSQLDRDEVAAISESAPTVVASGLSPELLPSLLAAVHRRRRRTRLITWVASSAAAAVLAIGVLVGVQGHSAAPQRAAVSALPMAQVGTQLLASTVSISGEPWGTFINLRCVCLAPPYASHDTLAMVVVGRDGSQTRLATWLAEPGHTATPAGSISTPVDQIAAVQVVAADTGQVLLQRSL
Enzyme Length 250
Uniprot Accession Number P9WJ66
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF) sigma factor SigL. ECF sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal 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, Rip1), while cytoplasmic proteases finish degrading the regulatory protein, liberating the sigma factor (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Metal binding (4); Topological domain (2); Transmembrane (1)
Keywords Cell membrane;Membrane;Metal-binding;Transcription;Transcription regulation;Transmembrane;Transmembrane helix;Virulence;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-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 25,938
Kinetics
Metal Binding METAL 25; /note=Zinc; via tele nitrogen; /evidence=ECO:0000250; METAL 50; /note=Zinc; via tele nitrogen; /evidence=ECO:0000250; METAL 54; /note=Zinc; /evidence=ECO:0000250; METAL 57; /note=Zinc; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda