Regulator of sigma-E protease RseP

UniProtKB accession:  P0AEH1

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UniProtKB description:  A site-2 regulated intramembrane protease (S2P) that cleaves the peptide bond between 'Ala-108' and 'Cys-109' in the transmembrane region of RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. Acts on DegS-cleaved RseA to release the cytoplasmic domain of RseA, residue 'Val-148' of RseA may be required for this. This provides the cell with sigma-E (RpoE) activity through the proteolysis of RseA. Can also cleave sequences in transmembrane regions of other proteins (such as LacY) as well as liberated signal peptides of beta-lactamase, OmpF, LivK, SecM, PhoA, LivJ, OmpC, Lpp and TorA, probably within the membrane. Cleaves FecR within its transmembrane region to release an N-terminal cytoplasmic fragment which binds to sigma factor FecI, allowing it to activate transcription of the fecABCDE operon which mediates ferric citrate transport (PubMed:33865858).