In secondary active transport, lactose permease in E. coli utilizes:
Secondary active lactose permease LacY does not itself hydrolyze ATP nor perform direct phosphorylation of sugar substrate like phosphotransferase systems that import glucose as glucose-6-phosphate. Instead energy source is electrochemical proton gradient across E. coli inner membrane established by respiratory chain proton pumping. Lactose entry is strictly coupled to downhill H+ flow: one proton symported per lactose disaccharide. Experimental evidence shows that abolishing proton motive force with uncouplers carbonyl cyanide m-chlorophenyl hydrazone, nigericin, or by inhibiting respiration
Ref: Kaback et al., J Gen Physiol 2008, Proton coupling LacY; Poolman et al., Mol Microbiol 2004.