%0 Journal Article %A Chenault, Sara S. %A Earhart, Charles F. %T Identification of hydrophobic proteins FepD and FepG of the Escherichia coli ferrienterobactin permease %D 1992 %J Microbiology, %V 138 %N 10 %P 2167-2171 %@ 1465-2080 %R https://doi.org/10.1099/00221287-138-10-2167 %I Microbiology Society, %X In Escherichia coli, iron assimilation by means of the siderophore enterobactin requires two hydrophobic cytoplasmic membrane proteins, FepD and FepG, which are essential components of a binding-protein-dependent transport system. Such components are typically difficult to detect. Here we report observation of the fepD and fepG gene products in polyacrylamide gels; they appeared as diffuse bands at positions consistent with smaller sizes than those predicted by sequence analysis. Translational coupling was suggested by the lack of a detectable product from the fepG message in the absence of translation of the upstream fepD message. The orientation of FepD/FepG in the membrane was predicted based on their similarities in sequence and hydrophobicity to FhuB. %U https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-138-10-2167