Uptake of ala in exponentially grown and starved cells of Escherichia coli B/r is inhibited by monochromatic far–UV (254–310 nm) and near UV (310–405 nm) light. The action spectrum for inhibition of ala uptake is similar to that found earlier for gly uptake, showing a maximum at 280 nm and a significant but much lower action throughout the near–UV region. The action spectra suggest that the chromophores for inactivation of ala and gly uptake lie in the carrier proteins and that these proteins are similar. Kinetic studies, in unirradiated bacteria, show that (a) the Km for ala uptake (11 μM) is about twice that for gly uptake (4.9 μM), (b) the Km for ala uptake does not change in the presence of gly, although the Kmax does decrease, and (c) other amino acids, such as ser and phe, have no effect on the Km or Vmax of the ala uptake system. These data suggest that ala and gly are transported by the same carrier protein, with the binding sites for ala and gly on different subunits.