The selectivity filter of K + channels is conserved throughout all kingdoms of life. Carbonyl groups of highly conserved amino acids point toward the lumen to act as surrogates for the water molecules of K + hydration. Ion conductivity is abrogated if some of these carbonyl groups flip out of the lumen, which happens (i) in the process of C-type inactivation or (ii) during filter collapse in the absence of K + . Here, we show that K + channels remain permeable to water, even after entering such an electrically silent conformation. We reconstituted fluorescently labeled and constitutively open mutants of the bacterial K + channel KcsA into lipid vesicles that were either C-type inactivating or noninactivating. Fluorescence correlation spectroscopy allowed us to count both the number of proteoliposomes and the number of protein-containing micelles after solubilization, providing the number of reconstituted channels per proteoliposome. Quantification of the per-channel increment in proteoliposome water permeability with the aid of stopped-flow experiments yielded a unitary water permeability p f of (6.9 ± 0.6) × 10 −13 cm 3 ·s −1 for both mutants. "Collapse" of the selectivity filter upon K + removal did not alter p f and was fully reversible, as demonstrated by current measurements through planar bilayers in a K + -containing medium to which K + -free proteoliposomes were fused. Water flow through KcsA is halved by 200 mM K + in the aqueous solution, which indicates an effective K + dissociation constant in that range for a singly occupied channel. This questions the widely accepted hypothesis that multiple K + ions in the selectivity filter act to mutually destabilize binding. membrane channels | protein reconstitution | knock-on mechanism | aquaporin | brain water homeostasis