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Its mode of function is controversial; it has been proposed to be an mRNA interferase but also an inhibitor of translation initiation. When overproduced in wild-type cells, inhibits bacterial growth and translation by cleavage of mRNA molecules while it has a weak effect on colony forming ability. Overproduction of Lon protease specifically activates YoeB-dependent mRNA cleavage, leading to lethality. YefM binds to the promoter region of the yefM-yeoB operon to repress transcription, YeoB acts as a corepressor"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16109374"}],"value":"Shown in vitro to be an mRNA interferase that requires translation for substrate cleavage; if the mRNA is mutated so as to not be translatable it is no longer cleaved. Cleavage only occurs within translated regions. 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Binds the 50S ribosomal subunit"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16768798"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17170003"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19400780"}],"value":"Repressed by YefM, more strongly repressed by the YefM(2)YoeB heterotrimer. Induced in persister cells. Ectopic expression of Salmonella or Shigella toxin VapC induces the yefM-yoeB operon and also induces Yoeb toxin activity in a Lon protease-dependent manner"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15009896"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16768798"}],"value":"No visible phenotype under standard growth conditions. Delays Lon protease-dependent lethality upon overexpression of Lon, but does not fully suppress it. 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