Detail Information for IndEnz0002001937
IED ID IndEnz0002001937
Enzyme Type ID protease001937
Protein Name Anti-sigma-L factor RslA
Regulator of SigL
Sigma-L anti-sigma factor RslA
Gene Name rslA Rv0736
Organism Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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 25618 / H37Rv)
Enzyme Sequence MTMPLRGLGPPDDTGVREVSTGDDHHYAMWDAAYVLGALSAADRREFEAHLAGCPECRGAVTELCGVPALLSQLDRDEVAAISESAPTVVASGLSPELLPSLLAAVHRRRRRTRLITWVASSAAAAVLAIGVLVGVQGHSAAPQRAAVSALPMAQVGTQLLASTVSISGEPWGTFINLRCVCLAPPYASHDTLAMVVVGRDGSQTRLATWLAEPGHTATPAGSISTPVDQIAAVQVVAADTGQVLLQRSL
Enzyme Length 250
Uniprot Accession Number P9WJ67
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. {ECO:0000269|PubMed:16552079}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Helix (6); Metal binding (4); Mutagenesis (2); Topological domain (2); Transmembrane (1)
Keywords 3D-structure;Cell membrane;Membrane;Metal-binding;Reference proteome;Transcription;Transcription regulation;Transmembrane;Transmembrane helix;Virulence;Zinc
Interact With
Induction INDUCTION: Constitutively expressed from a very weak SigL-independent promoter during growth in culture. Also weakly autoregulated. Forms an operon with sigL. {ECO:0000269|PubMed:16199577}.
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 3HUG;
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 25,938
Kinetics
Metal Binding METAL 25; /note=Zinc; via tele nitrogen; /evidence=ECO:0000269|PubMed:20184899; METAL 50; /note=Zinc; via tele nitrogen; /evidence=ECO:0000269|PubMed:20184899; METAL 54; /note=Zinc; /evidence=ECO:0000269|PubMed:20184899; METAL 57; /note=Zinc; /evidence=ECO:0000269|PubMed:20184899
Rhea ID
Cross Reference Brenda