IED ID | IndEnz0002008268 |
Enzyme Type ID | protease008268 |
Protein Name |
Anti-sigma-K factor RskA Regulator of SigK Sigma-K anti-sigma factor RskA |
Gene Name | rskA Mkms_4459 |
Organism | Mycobacterium sp. (strain KMS) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium unclassified Mycobacterium Mycobacterium sp. (strain KMS) |
Enzyme Sequence | MTEPNNTDLLDLATPYALHAVSIDERFEIDRWLATAPPEVADAFTDEVRSVQETMAVLSAATATEPPAHLRDNVLAMVADDPVRDLGSARRRRGGESRWRTAVLAAAAVAVVGLGALGVGLALRPAVSPTTADQVFAAPDVQTVSGPIPGGGTATVVFSKERDAGVLVMNDVAPPKPGTVYQMWLVGSDGPHSAGTMDDKAISPSTTAVLSDIGTSQALAFTVEPPGGSQRPTSPAFAELPLT |
Enzyme Length | 243 |
Uniprot Accession Number | A1ULE2 |
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); Region (1); Topological domain (2); Transmembrane (1) |
Keywords | Cell membrane;Membrane;Reference proteome;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 | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 25,147 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |