| IED ID | IndEnz0002008978 |
| Enzyme Type ID | protease008978 |
| 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 STM14_3233 |
| 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 | MQKEKLSALMDGETLDSELLKALTHDPEMQKTWESYHLIRDSMRGDTPDVLHFDISARVMAAIENEPVRQVSPLIPEAQPAPQQWQKMPFWKKVRPWAAQLTQMGVAACVSLAVIVGVQHYNGQSETSQQPETPVFNTLPMMGKASPVSLGVPSEAAPVGSQQQQVQEQRRRINAMLQDYELQRRLHSEQLQFEQAQTQQAAVQVPGIQTLGTQSQ |
| Enzyme Length | 216 |
| Uniprot Accession Number | D0ZSY8 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Responds differently to heat shock versus acid shock; degradation in response to heat shock requires sequential DegS and RseP action, whereas degradation in response to acid shock requires only RseP. {ECO:0000269|PubMed:19170886}. |
| 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 (periplasmic or acid stress or heat shock) 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 (Probable). In this organism acid stress response does not require DegS degradation. {ECO:0000269|PubMed:19170886, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Coiled coil (1); Region (1); Site (2); Topological domain (2); Transmembrane (1) |
| Keywords | Cell inner membrane;Cell membrane;Coiled coil;Membrane;Signal-anchor;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. |
| 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 (Probable). {ECO:0000305}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 24,223 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |