| IED ID | IndEnz0002008412 |
| Enzyme Type ID | protease008412 |
| Protein Name |
ECF RNA polymerase sigma-E factor RNA polymerase sigma-E factor |
| Gene Name | rpoE sigE STM14_3234 |
| Organism | Salmonella typhimurium (strain 14028s / SGSC 2262) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Salmonella Salmonella enterica (Salmonella choleraesuis) Salmonella enterica I Salmonella typhimurium Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) Salmonella typhimurium (strain 14028s / SGSC 2262) |
| Enzyme Sequence | MSEQLTDQVLVERVQKGDQKAFNLLVVRYQHKVASLVSRYVPSGDVPDVVQESFIKAYRALDSFRGDSAFYTWLYRIAVNTAKNYLVAQGRRPPSSDVDAIEAENFESGGALKEISNPENLMLSEELRQIVFRTIESLPEDLRMAITLRELDGLSYEEIAAIMDCPVGTVRSRIFRAREAIDNKVQPLIRR |
| Enzyme Length | 191 |
| Uniprot Accession Number | D0ZSY9 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: ECF sigma-E is held in an inactive form by its cognate anti-sigma factor (RseA) until released by regulated intramembrane proteolysis (RIP). RIP occurs when an extracytoplasmic signal (periplasmic, acid or heat stress) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. In S.typhimurium there are 2 cascades, the heat shock response which depends on DegS and RseP, and acid response which depends only on RseP. The anti-sigma factor RseA is an inner membrane protein, binding sigma-E in the cytoplasm and RseB in the periplasm. RseA is first cut extracytoplasmically (site-1 protease, S1P, by DegS), then within the membrane itself (site-2 protease, S2P, by RseP), while cytoplasmic proteases (predominantly ClpX-ClpP) finish degrading the regulatory protein, liberating sigma-E. Degradation of RseA requires 2 signals to activate DegS; an outer membrane protein (OMP) signal activates DegS, while an LPS signal causes release of RseB from RseA, freeing RseA to be cleaved. OMP stress can be abrogated by overexpression of the sRNA rybB. {ECO:0000269|PubMed:19170886}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | DNA_BIND 156..175; /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 (RNAP) to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment. {ECO:0000269|PubMed:19170886}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); DNA binding (1); Motif (1); Region (3) |
| Keywords | Cytoplasm;DNA-binding;Sigma factor;Stress response;Transcription;Transcription regulation;Virulence |
| Interact With | |
| Induction | INDUCTION: Poorly expressed in logarithmic growth, induced in stationary phase. By acid stress (pH 4.5), heat shock. Has 3 promoters, the first 2 are sigma-70-dependent, the third is positively auto-regulated. {ECO:0000269|PubMed:11929531, ECO:0000269|PubMed:19170886}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=Associates with the inner membrane via RseA. {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 48..61; /note=Polymerase core binding |
| Gene Encoded By | |
| Mass | 21,712 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |