| IED ID | IndEnz0002009535 |
| Enzyme Type ID | protease009535 |
| Protein Name |
ECF RNA polymerase sigma factor SigD ECF sigma factor SigD Alternative RNA polymerase sigma factor SigD RNA polymerase sigma-D factor Sigma-D factor |
| Gene Name | sigD Rv3414c MTCY78.15 |
| 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 | MVDPGVSPGCVRFVTLEISPSMTMQGERLDAVVAEAVAGDRNALREVLETIRPIVVRYCRARVGTVERSGLSADDVAQEVCLATITALPRYRDRGRPFLAFLYGIAAHKVADAHRAAGRDRAYPAETLPERWSADAGPEQMAIEADSVTRMNELLEILPAKQREILILRVVVGLSAEETAAAVGSTTGAVRVAQHRALQRLKDEIVAAGDYA |
| Enzyme Length | 212 |
| Uniprot Accession Number | P9WGG9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | DNA_BIND 176..195; /note=H-T-H motif; /evidence=ECO:0000250 |
| EC Number | |
| Enzyme Function | FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor until released by regulated intramembrane proteolysis. {ECO:0000269|PubMed:15375142}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); DNA binding (1); Helix (4); Motif (1); Region (2) |
| Keywords | 3D-structure;DNA-binding;Reference proteome;Sigma factor;Transcription;Transcription regulation;Virulence |
| Interact With | |
| Induction | INDUCTION: Positively autoregulates, probably directly, expressed at a relatively high level throughout exponential growth and during stationary phase. Expression decreases during O(2) depletion (hypoxia) (PubMed:15375142) and after heat shock (5-fold, 45 degrees Celsius) (PubMed:10027986). {ECO:0000269|PubMed:10027986, ECO:0000269|PubMed:15375142}. |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 3VEP; 3VFZ; |
| Mapped Pubmed ID | - |
| Motif | MOTIF 75..78; /note=Polymerase core binding; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 22,919 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |