| 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 |