| IED ID | IndEnz0002009118 | 
| Enzyme Type ID | protease009118 | 
| Protein Name | 
                        
                            
                                Anti-sigma-K factor RskA  Regulator of SigK Sigma-K anti-sigma factor RskA  | 
                    
| Gene Name | rskA Rv0444c | 
| 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 | MTEHTDFELLELATPYALNAVSDDERADIDRRVAAAPSPVAAAFNDEVRAVRETMAVVSAATTAEPPAHLRTAILDATKPEVRRQSRWRTAAFASAAAIAVGLGAFGLGVLTRPSPPPTVAEQVLTAPDVRTVSRPLGAGTATVVFSRDRNTGLLVMNNVAPPSRGTVYQMWLLGGAKGPRSAGTMGTAAVTPSTTATLTDLGASTALAFTVEPGTGSPQPTGTILAELPLG | 
| Enzyme Length | 232 | 
| Uniprot Accession Number | P9WGX5 | 
| 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. {ECO:0000269|PubMed:17064366}. | 
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Helix (6); Initiator methionine (1); Modified residue (1); Topological domain (2); Transmembrane (1) | 
| Keywords | 3D-structure;Acetylation;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 | MOD_RES 2; /note=N-acetylthreonine; /evidence=ECO:0007744|PubMed:21969609 | 
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) | 
| Cross Reference PDB | 4NQW; | 
| Mapped Pubmed ID | 24699647; | 
| Motif | |
| Gene Encoded By | |
| Mass | 23,883 | 
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |