Ludwig W, Kaim G, Laubinger W, Dimroth P, Hoppe J, Schleifer K H
Lehrstuhl für Mikrobiologie, Technische Universität München, Federal Republic of Germany.
Eur J Biochem. 1990 Oct 24;193(2):395-9. doi: 10.1111/j.1432-1033.1990.tb19352.x.
The 30 N-terminal amino acid residues of the purified ATPase c subunit of Propionigenium modestum have been determined. An oligonucleotide mixture was derived from this sequence and used as probe for cloning the corresponding gene in Escherichia coli. The nucleotide sequence of the gene has been determined and compared with those of ATPase c subunits from other bacteria and chloroplasts. Peculiar sequence similarities are found only at the C-terminus between the c subunits of the ATPases from P. modestum and from Vibrio alginolyticus, another putative Na(+)-translocating ATPase.