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Thermophilic enzymes can operate at higher temperatures but show reducedactivities at room temperature. They are in general more stable duringpreparation and, accordingly, are considered to be more rigid in structure.Crystallization is often easier compared to proteins from bacteria growing atambient temperatures, especially for membrane proteins. The ATP-producingenzyme FoF1-ATP synthase from thermoalkaliphilic Caldalkalibacillus thermarumstrain TA2.A1 is driven by a Fo motor consisting of a ring of 13 c-subunits. Weapplied a single-molecule F\"orster resonance energy transfer (FRET) approachusing duty cycle-optimized alternating laser excitation (DCO-ALEX) to monitorthe expected 13-stepped rotary Fo motor at work. New FRET transition histogramswere developed to identify the smaller step sizes compared to the 10-stepped Fomotor of the Escherichia coli enzyme. Dwell time analysis revealed thetemperature and the LDAO dependence of the Fo motor activity on the singlemolecule level. Back-and-forth stepping of the Fo motor occurs fast indicatinga high flexibility in the membrane part of this thermophilic enzyme.

Step size of the rotary proton motor in single FoF1-ATP synthase from a thermoalkaliphilic bacterium by DCO-ALEX FRET