Detail Information for IndEnz0002010791
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