Analysis of the flagellin (hag) gene of alkalophilic Bacillus sp. C-125.
Motility of the alkalophilic Bacillus sp. C-125, a flagellate bacterium, was demonstrated to be Na(+)- and pH-dependent. Flagellin protein from this strain was purified to homogeneity and the N-terminal sequence determined. Using the hag gene of Bacillus subtilis as a probe, the hag gene of Bacillus sp. C-125 was identified and cloned into Escherichia coli. Sequencing of this hag gene revealed that it encodes a protein of 272 amino acids (M(r) 29,995). The predicted N terminal sequence of this protein was identical to that determined by N-terminal sequencing of the flagellin protein from strain C-125. The alkalophilic Bacillus sp. C-125 flagellin shares homology with other known flagellins in both the N- and C-terminal regions. The middle portion, however, shows considerable differences, even from that of flagellin from the related species, B. subtilis.
Sakamoto
Y
Y
The RIKEN Institute, Saitama, Japan.
Sutherland
K J
KJ
Tamaoka
J
J
Kobayashi
T
T
Kudo
T
T
Horikoshi
K
K
D000595:Amino Acid Sequence; D001407:Bacillus / Q000235:genetics*; D001483:Base Sequence; D002465:Cell Movement / Q000187:drug effects / Q000235:genetics*; D005408:Flagellin / Q000235:genetics*; D005798:Genes, Bacterial / Q000235:genetics*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D015183:Restriction Mapping; D017386:Sequence Homology, Amino Acid; D012964:Sodium / Q000494:pharmacology
D005408:Flagellin; D012964:Sodium