The A-type ATP synthase subunit K of Methanopyrus kandleri is deduced from its sequence to form a monomeric rotor comprising 13 hairpin domains.
The ntpK gene of the archaeon Methanopyrus kandleri encodes the equivalent of the c subunit of ATP synthase. The gene product contains 1021 residues and consists of 13 homologous domains, each one corresponding to a single helical hairpin. The amino acid sequence of the domains is highly conserved, ranging between 50 and 80% sequence identity. Each of the 13 domains contains a conserved Gln and Glu residue in the N- and C-terminal helix, respectively, both of which are believed to be involved in cation binding. The protein is likely to form the monomeric rotor of the ATP synthase that consists of 13 hairpin domains.
Lolkema
Juke S
JS
Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN, Haren, The Netherlands. j.s.lolkema@biol.rug.nl
Boekema
Egbert J
EJ
D000595:Amino Acid Sequence; D025243:Bacterial Proton-Translocating ATPases / Q000737:chemistry*; D019605:Euryarchaeota / Q000201:enzymology*; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D016415:Sequence Alignment; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry
D021122:Protein Subunits; D025243:Bacterial Proton-Translocating ATPases; D025262:Vacuolar Proton-Translocating ATPases