Mutant deletions in Escherichia coli affect the cellular levels of undecaprenyl phosphate and undecaprenyl diphosphate

wild type strain W3110; in the YS1234 strain defective in ynbD, yeiU, ybjG, and pgpB; in the YS1235 strain defective in ynbD, yeiU, ybjG, and bacA; and in the YS1245 strain defective in ynbD, yeiU, pgpB, and bacA were 78.0% ± 3.5%, 74.7% ± 1.2%, 68.4% ± 6.8%, and 64.0% ± 7.5%, respectively. The quadruple mutant strain that possessed the wild-type bacA showed almost identical UP level as the wild type strain W3110, indicating that sufficient level of UPP phosphatse activity was conferred by a bacA product without the products of ynbD, yeiU, ybjG, and pgpB. However, the mutants defective in bacA showed a slight but significant (p < 0.01) decrease in the UP level.