IED ID | IndEnz0002010791 |
Enzyme Type ID | protease010791 |
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 HI_0629 |
Organism | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pasteurellales Pasteurellaceae Haemophilus Haemophilus influenzae Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
Enzyme Sequence | MQKEQLSAYMDGEQVETDLIDALLRDEELQASWHSFHTVRSVMRKESAVFLGADFTAKMADLIELEDVKKVDVIAVSQPEPEDAHNSVFMQKLKAFFAPMTQVAVAAGVCLVAVLGVQSFNNKNDASNLPETPVLQTLPFNNAVQEVSYNAPSKDTLTSDQLEKKSRRIGAMLQNYELQRRMHSDALDVSSSQVR |
Enzyme Length | 195 |
Uniprot Accession Number | P44791 |
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 (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Coiled coil (1); Site (1); Topological domain (2); Transmembrane (1) |
Keywords | Cell inner membrane;Cell membrane;Coiled coil;Membrane;Reference proteome;Signal-anchor;Transcription;Transcription regulation;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Following cleavage by DegS the large fragment of the protein is still in the inner membrane and retains its anti-sigma-E activity. {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | PTM: Sequentially cleaved by DegS (a site-1 protease) in its periplasmic domain between Val-147 and Ser-148, then by RseP (a site-2 protease). 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 (By similarity). {ECO:0000250}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 21,733 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |