biostudies-literatureYokoyama TMEXT | Japan Society for the Promotion of ScienceMEXT | Japan Society for the Promotion of Science (JSPS)Institute for Fermentation, Osaka (IFO)Platform Project for Supporting in Drug Discovery and Life Science Research form the Japan Agency for Medical Research and DevelopmentCooperative Research Program (Joint Usage/Research Centerprogram) of the Institute for Frontier Life and Medical Sciences Kyoto UniversityInstitute for Fermentation, OsakaInstitute for Frontier Life and Medical Sciences, Kyoto University for INFRONT Office of Director's Research Grant Program (2021)Institute for Frontier Life and Medical Sciences, Kyoto University for INFRONT Office of Director&apos;s Research Grant ProgramInstitute for Frontier Life and Medical Sciences, Kyoto University for INFRONT Office of Director's Research Grant Program (2020)e0108623https://www.ebi.ac.uk/biostudies/studies/S-EPMC10470546biostudies-literatureUnknown14(4)The site2<i>-</i>protease (S2P) family of intramembrane proteases (IMPs) is conserved in all kingdoms of life and cleaves transmembrane proteins within the membrane to regulate and maintain various cellular activities. RseP, an <i>Escherichia coli</i> S2P peptidase, is involved in the regulation of gene expression through the regulated cleavage of the two target membrane proteins (RseA and FecR) and in membrane quality control through the proteolytic elimination of remnant signal peptides. RseP is expected to have additional substrates and to be involved in other cellular processes. Recent studies have shown that cells express small membrane proteins (SMPs; single-spanning membrane proteins of approximately 50-100 amino acid residues) with crucial cellular functions. However, little is knomBioS2P intramembrane protease RseP degrades small membrane proteins and suppresses the cytotoxicity of intrinsic toxin HokB.PMC10470546JP26291016G-2022-2-108JP22H02571JP22H02561JP21J15841JP18H02404N.A.JP22K06142JP16am0101020JP19K06562JP19H03170Yokoyama THonna SNogi TAkiyama YMizuno SKatagiri SHizukuri YOi RYamagata YfalseS2P intramembrane protease RseP degrades small membrane proteins and suppresses the cytotoxicity of intrinsic toxin HokB.The site2<i>-</i>protease (S2P) family of intramembrane proteases (IMPs) is conserved in all kingdoms of life and cleaves transmembrane proteins within the membrane to regulate and maintain various cellular activities. RseP, an <i>Escherichia coli</i> S2P peptidase, is involved in the regulation of gene expression through the regulated cleavage of the two target membrane proteins (RseA and FecR) and in membrane quality control through the proteolytic elimination of remnant signal peptides. RseP is expected to have additional substrates and to be involved in other cellular processes. Recent studies have shown that cells express small membrane proteins (SMPs; single-spanning membrane proteins of approximately 50-100 amino acid residues) with crucial cellular functions. However, little is kno2023-01-01T00:00:00Z2023 Aug2025-04-19T20:05:46.896Z2025-04-19T20:05:46.896ZS-EPMC104705463740981010.1128/mbio.01086-23