FEATURES

FAMILY

DESCRIPTION

Also known as RSEP_ECOLI, rseP, ecfE, yaeL. 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. Interacts with RseA; the third transmembrane domain can be cross-linked to the transmembrane domain of RseA.

EXTERNAL LINKS

rseP

Regulator of sigma-E protease RseP

rseP

Molecular Synopsis