| IED ID | IndEnz0002010606 |
| Enzyme Type ID | protease010606 |
| Protein Name |
ECF RNA polymerase sigma-E factor RNA polymerase sigma-E factor Sigma-24 |
| Gene Name | rpoE sigE b2573 JW2557 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MSEQLTDQVLVERVQKGDQKAFNLLVVRYQHKVASLVSRYVPSGDVPDVVQEAFIKAYRALDSFRGDSAFYTWLYRIAVNTAKNYLVAQGRRPPSSDVDAIEAENFESGGALKEISNPENLMLSEELRQIVFRTIESLPEDLRMAITLRELDGLSYEEIAAIMDCPVGTVRSRIFRAREAIDNKVQPLIRR |
| Enzyme Length | 191 |
| Uniprot Accession Number | P0AGB6 |
| 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 stress and excess LPS) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. 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 (PubMed:15371343). 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 (PubMed:23687042). The rate-limiting step in this protease cascade is the first signal-sensing cleavage (half-life about 1 minute) (PubMed:17210793). {ECO:0000269|PubMed:15371343, ECO:0000269|PubMed:17210793, ECO:0000269|PubMed:23687042, ECO:0000269|PubMed:9159522}. |
| 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 (PubMed:7889935, PubMed:2691330, PubMed:9159522, PubMed:9159523). Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as heat shock (PubMed:7889935) and oxidative stress; it controls protein processing in the extracytoplasmic compartment. The 90 member regulon consists of the genes necessary for the synthesis and maintenance of both proteins and LPS of the outer membrane (PubMed:7889934, PubMed:11274153, PubMed:16336047). Indirectly activates transcription of csrB and csrC, 2 sRNAs that antagonize translational regulator CsrA, linking envelope stress, the stringent response and the catabolite repression systems (PubMed:28924029). {ECO:0000269|PubMed:11274153, ECO:0000269|PubMed:16336047, ECO:0000269|PubMed:2691330, ECO:0000269|PubMed:28924029, ECO:0000269|PubMed:7889934, ECO:0000269|PubMed:7889935, ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (2); Chain (1); DNA binding (1); Erroneous initiation (1); Helix (12); Motif (1); Mutagenesis (6); Region (3); Turn (1) |
| Keywords | 3D-structure;Cytoplasm;DNA-binding;Direct protein sequencing;Reference proteome;Sigma factor;Stress response;Transcription;Transcription regulation |
| Interact With | Q46864 |
| Induction | INDUCTION: Induced after shifting to 50 degrees Celsius (at protein level) (PubMed:2691330). Induced when the level of outer membrane proteins (OMP) increases (at protein level) (PubMed:8276244, PubMed:10500101). Induced as periplasmic levels of LPS levels increase (PubMed:23687042). Induced by misfolded periplasmic proteins (PubMed:9351822). Transcription positively autoregulated (via promoter P2) (PubMed:7889935). Transcription slightly induced by elevated temperatures (PubMed:7889934). Transiently induced by cold shock in a PNPase-dependent fashion (PubMed:14527658). Translation repressed by CsrA which binds to 3 sites in the 5'-UTR which occludes the ribosome binding site (PubMed:28924029). Translation is coupled to upstream leader peptide RseD, whose stop codon overlaps with the start codon of rpoE; when coupling is eliminated translation is decreased by about 50% (PubMed:28924029). Part of the rseD-rpoE-rseA-rseB-rseC operon (PubMed:9159522, PubMed:9159523, PubMed:28924029). {ECO:0000269|PubMed:10500101, ECO:0000269|PubMed:14527658, ECO:0000269|PubMed:23687042, ECO:0000269|PubMed:2691330, ECO:0000269|PubMed:28924029, ECO:0000269|PubMed:7889934, ECO:0000269|PubMed:7889935, ECO:0000269|PubMed:8276244, ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523, ECO:0000269|PubMed:9351822}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:9159522}. Note=Associates with the inner membrane via RseA (PubMed:9159522, PubMed:11777003). {ECO:0000269|PubMed:11777003}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1); Electron microscopy (1); X-ray crystallography (2) |
| Cross Reference PDB | 1OR7; 2H27; 5OR5; 6JBQ; |
| Mapped Pubmed ID | 16606699; 19834901; 24531660; 24561554; 31131408; |
| Motif | MOTIF 48..61; /note=Polymerase core binding |
| Gene Encoded By | |
| Mass | 21,696 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |