Detail Information for IndEnz0002013054
IED ID IndEnz0002013054
Enzyme Type ID protease013054
Protein Name ECF RNA polymerase sigma-E factor
RNA polymerase sigma-E factor
Sigma-24
Gene Name rpoE sigE STY2833 t0270
Organism Salmonella typhi
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Salmonella Salmonella enterica (Salmonella choleraesuis) Salmonella enterica I Salmonella typhi
Enzyme Sequence MSEQLTDQVLVERVQKGDQKAFNLLVVRYQHKVASLVSRYVPSGDVPDVVQESFIKAYRALDSFRGDSAFYTWLYRIAVNTAKNYLVAQGRRPPSSDVDAIEAENFESGGALKEISNPENLMLSEELRQIVFRTIESLPEDLRMAITLRELDGLSYEEIAAIMDCPVGTVRSRIFRAREAIDNKVQPLIRR
Enzyme Length 191
Uniprot Accession Number P0A2F1
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. 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 (By similarity). {ECO:0000250}.
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. Extracytoplasmic function (ECF) sigma-E controls the envelope stress response, responding to periplasmic protein stress, increased levels of periplasmic lipopolysaccharide (LPS) as well as acid stress, heat shock and oxidative stress; it controls protein processing in the extracytoplasmic compartment (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); DNA binding (1); Motif (1); Region (3)
Keywords Cytoplasm;DNA-binding;Sigma factor;Stress response;Transcription;Transcription regulation
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Associates with the inner membrane via RseA. {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 48..61; /note=Polymerase core binding; /evidence=ECO:0000250
Gene Encoded By
Mass 21,712
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda