| IED ID | IndEnz0002008731 |
| Enzyme Type ID | protease008731 |
| Protein Name |
Anti-sigma-E factor RseA Regulator of SigE Sigma-E anti-sigma factor RseA Sigma-E factor negative regulatory protein |
| Gene Name | rseA mclA yfiJ b2572 JW2556 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MQKEQLSALMDGETLDSELLNELAHNPEMQKTWESYHLIRDSMRGDTPEVLHFDISSRVMAAIEEEPVRQPATLIPEAQPAPHQWQKMPFWQKVRPWAAQLTQMGVAACVSLAVIVGVQHYNGQSETSQQPETPVFNTLPMMGKASPVSLGVPSEATANNGQQQQVQEQRRRINAMLQDYELQRRLHSEQLQFEQAQTQQAAVQVPGIQTLGTQSQ |
| Enzyme Length | 216 |
| Uniprot Accession Number | P0AFX7 |
| 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 sigma-E (RpoE). 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 periplasmically (site-1 protease, S1P, DegS), then within the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic proteases finish degrading the anti-sigma factor, liberating sigma-E. Overexpression of RseA blocks sigma-E from acting, results in cell lysis in stationary phase and temperature-sensitivity above 37 degrees Celsius. {ECO:0000269|PubMed:23687042, ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (1); Chain (1); Coiled coil (1); Compositional bias (1); Frameshift (1); Helix (8); Mutagenesis (19); Region (4); Site (2); Topological domain (2); Transmembrane (1) |
| Keywords | 3D-structure;Cell inner membrane;Cell membrane;Coiled coil;Direct protein sequencing;Membrane;Reference proteome;Signal-anchor;Transcription;Transcription regulation;Transmembrane;Transmembrane helix |
| Interact With | P0AEE3; P0AFX9 |
| Induction | INDUCTION: Transiently induced by cold shock in a PNPase-dependent fashion. Upon stress induction (OMPs or heat shock) decreases in under 3 minutes (at protein level). 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:28924029, ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}; Single-pass type II membrane protein {ECO:0000269|PubMed:11777003, ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:9159522, ECO:0000269|PubMed:9159523}. Note=Following cleavage by DegS the large fragment of the protein is still in the inner membrane and retains its anti-sigma-E activity. |
| Modified Residue | |
| Post Translational Modification | PTM: Sequentially cleaved by DegS (a site-1 protease) in its periplasmic domain between Val-148 and Ser-149, then by RseP (a site-2 protease) between positions Ala-108 and Cys-109. The N-terminal fragment is then degraded by primarily ClpX-ClpP in an ATP-dependent fashion. Sequential cleavage by DegS, RseP and ClpX-ClpP frees RpoE from RseA. {ECO:0000269|PubMed:12183368, ECO:0000269|PubMed:12183369, ECO:0000269|PubMed:12679035, ECO:0000269|PubMed:14633997, ECO:0000269|PubMed:15371343, ECO:0000269|PubMed:15496982, ECO:0000269|PubMed:18268014, ECO:0000269|PubMed:18945679, ECO:0000269|PubMed:19706448, ECO:0000269|PubMed:23687042}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1OR7; 1YFN; 3M4W; |
| Mapped Pubmed ID | 11442831; 12670975; 16606699; 17981123; 19103591; 22885295; 24561554; |
| Motif | |
| Gene Encoded By | |
| Mass | 24,321 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |