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The  c  ring of the Na +  F 1 F o  ATP synthase from the anaerobic acetogenic bacterium  Acetobacterium woodii  is encoded by three different genes:  atpE  1 ,  atpE  2  and  atpE  3 . Subunit  c  1  is similar to typical V-type  c  subunits and has four transmembrane helices with one ion binding site. Subunit  c  2  and  c  3  are identical at the amino acid level and are typical F-type  c  subunits with one ion binding site in two transmembrane helices. All three constitute a hybrid F o V o  c  ring, the first found in nature. To analyze whether other species may have similar hybrid rotors, we searched every genome sequence publicly available as of 23 February 2015 for F 1 F o  ATPase operons that have more than one gene encoding the  c  subunit. This revealed no other species that has three different  c  subunit encoding genes but twelve species that encode one F o - and one V o -type  c  subunit in one operon. Their  c  subunits have the conserved binding motif for Na + . The organisms are all anaerobic. The advantage of hybrid  c  rings for the organisms in their environments is discussed.

Hybrid rotors in F 1 F o ATP synthases: subunit composition, distribution, and physiological significance