IED ID | IndEnz0002001325 |
Enzyme Type ID | protease001325 |
Protein Name |
Anti-sigma-D factor RsdA Regulator of SigD Sigma-D anti-sigma factor RsdA |
Gene Name | rsdA Rv3413c MTCY78.16 |
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 | MREFGNPLGDRPPLDELARTDLLLDALAEREEVDFADPRDDALAALLGQWRDDLRWPPASALVSQDEAVAALRAGVAQRRRARRSLAAVGSVAAALLVLSGFGAVVADARPGDLLYGLHAMMFNRSRVSDDQIVLSAKANLAKVEQMIAQGQWAEAQDELAEVSSTVQAVTDGSRRQDLINEVNLLNTKVETRDPNATLRPGSPSNPAAPGSVGNSWTPLAPVVEPPTPPTPASAAEPSMSAGVSESPMPNSTSTVAASPSTPSSKPEPGSIDPSLEPADEATNPAGQPAPETPVSPTH |
Enzyme Length | 299 |
Uniprot Accession Number | P9WJ71 |
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 SigD. 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), while cytoplasmic proteases finish degrading the regulatory protein, liberating the sigma factor. Neither S1P nor S2P proteases have been so far identified for this anti-sigma factor. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Compositional bias (2); Helix (2); Mutagenesis (2); Region (2); Topological domain (2); Transmembrane (1) |
Keywords | 3D-structure;Cell membrane;Membrane;Reference proteome;Transcription;Transcription regulation;Transmembrane;Transmembrane helix |
Interact With | |
Induction | INDUCTION: Positively regulated by alternative sigma factor SigD. {ECO:0000269|PubMed:15375142}. |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | PTM: The cytosolic fragment (residues 1-94) in both free and SigD-associated form, is degraded by a ClpP1-ClpP2-ClpX complex, as would be expected after S1P and S2P intramembrane proteolysis. This releases SigD so that it may bind to the RNA polymerase catalytic core. |
Signal Peptide | |
Structure 3D | X-ray crystallography (1) |
Cross Reference PDB | 3VEP; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 31,248 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |