Detail Information for IndEnz0002009116
IED ID IndEnz0002009116
Enzyme Type ID protease009116
Protein Name Anti-sigma-K factor RskA
Regulator of SigK
Sigma-K anti-sigma factor RskA
Gene Name rskA ERDMAN_0487
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 MTEHTDFELLELATPYALNAVSDDERADIDRRVAAAPSPVAAAFNDEVRAVRETMAVVSAATTAEPPAHLRTAILDATKPEVRRQSRWRTAAFASAAAIAVGLGAFGLGVLTRPSPPPTVAEQVLTAPDVRTVSRPLGAGTATVVFSRDRNTGLLVMNNVAPPSRGTVYQMWLLGGAKGPRSAGTMGTAAVTPSTTATLTDLGASTALAFTVEPGTGSPQPTGTILAELPLG
Enzyme Length 232
Uniprot Accession Number H8EVS9
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 SigK. 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); Topological domain (2); Transmembrane (1)
Keywords Cell membrane;Membrane;Transcription;Transcription regulation;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Modified Residue
Post Translational Modification PTM: Probably cleaved within the membrane by Rip1 near the cytoplasmic membrane interface.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 23,883
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda