Two high-affinity K+ uptake systems, KtrI and KtrII, have been reported in
Enterococcus hirae. A mutant, JEMK1, defective in these two systems did not
grow at pH 10 in low-K+ medium (less than 1 mM K+), but grew well when sup
plemented with 10 mM KCl. In this mutant. we found an energy-dependent K+ u
ptake at pH 10 with a low affinity for K+ (K-m of similar to 20 mM) and an
extremely high rate [V-max of 1.6 mu mol min(-1) (mg protein)(-1)]. Rb+ upt
ake [K-m of similar to 40 mM and V-max of 0.5 mu mol min(-1) (mg protein)(-
1), which was inhibited competitively by Ki and less prominently by Cs+, wa
s also observed. The specificity of this transport is likely to be K+>Rb+>C
s+. This peculiar K+ transport plays a role as a salvage mechanism against
defects in high-affinity systems in the K+ homeostasis of this bacterium.