Open AccessOn the Amino-Acid Sequence of Flagellin from Bacillus subtilis 168: Comparison with Other Bacterial Flagellins
Author(s) -
Robert J. DeLange,
Joyce Y. Chang,
Joël H. Shaper,
Rafael Martı́nez,
Stanley K. Komatsu,
Alexander N. Glazer
Publication year - 1973
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.70.12.3428
Subject(s) - flagellin , bacillus subtilis , residue (chemistry) , peptide sequence , homology (biology) , peptide , biochemistry , amino acid , biology , chemistry , microbiology and biotechnology , bacteria , genetics , gene
A partial amino-acid sequence ofBacillus subtilis 168 flagellin is presented. The region of unassigned sequence in this 304-residue polypeptide chain spans residues 158-173. Comparison of the 27-residue aminoterminal CNBr peptide ofB. subtilis 168 flagellin with that derived from the flagellin of the serologically unrelated strain ofB. subtilis , W23, shows only three conservative substitutions, whereas the 16-residue carboxyl-terminal peptides derived from these flagellins were identical. The comparison of the very limited sequence information available on the flagellins ofSalmonella andProteus with that onB. subtilis indicates homology between these proteins.