title: Molecular cloning of A1-ATPase gene from extremely halophilic archaeon Haloarcula japonica strain TR-1.
abstract: The genes encoding A1-ATPase A- and B-subunits were cloned from Haloarcula japonica strain TR-1. Nucleotide sequencing analysis of the A1-ATPase gene revealed that the A- and B-subunits consisted of 586 and 473 amino acids, respectively. The deduced amino acid sequences of the A- and B-subunits of Ha. japonica showed high identities with those of Halobacterium salinarum and Haloferax volcanii. The consensus ATP-binding motif was found in the A-subunit.
authors.affiliation: Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
authors.forename: R
authors.initials: R
authors.lastname: Yatsunami
authors.forename: M
authors.initials: M
authors.lastname: Iwamoto
authors.forename: K
authors.initials: K
authors.lastname: Ihara
authors.forename: S
authors.initials: S
authors.lastname: Nakamura
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000235:genetics*; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D019766:Genes, Archaeal; D019613:Haloarcula / Q000201:enzymology* / Q000235:genetics*; D019617:Halobacterium salinarum / Q000235:genetics; D019622:Haloferax volcanii / Q000235:genetics; D006358:Hot Temperature; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D016415:Sequence Alignment
chemical_list: D046911:Macromolecular Substances; D000251:Adenosine Triphosphatases