Cloning, expression, and nucleotide sequence of the alpha-amylase gene from the haloalkaliphilic archaeon Natronococcus sp. strain Ah-36.
The alpha-amylase gene of a Natronococcus sp. (1,512 bp) contained a signal peptide of 43 amino acids. Haloferax volcanii expressed the gene and cleaved the signal peptide accurately. The signal peptide shared an extremely high amino acid sequence identity with that of a protease from the halophilic archaeon 172P1.
Kobayashi
T
T
Laboratory of Microbiology, Institute of Physical and Chemical Research, Saitama, Japan.
Kanai
H
H
Aono
R
R
Horikoshi
K
K
Kudo
T
T
D000595:Amino Acid Sequence; D001105:Archaea / Q000201:enzymology / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes / Q000737:chemistry; D021382:Protein Sorting Signals / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry; D000516:alpha-Amylases / Q000235:genetics*
D015345:Oligonucleotide Probes; D021382:Protein Sorting Signals; D000516:alpha-Amylases; D012697:Serine Endopeptidases; C088712:halolysin