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. 1973 Dec;70(12 Pt 1-2):3428–3431. doi: 10.1073/pnas.70.12.3428

On the Amino-Acid Sequence of Flagellin from Bacillus subtilis 168: Comparison with Other Bacterial Flagellins

Robert J Delange *, Joyce Y Chang *,†, Joel H Shaper ‡,§, Rafael J Martinez ‡, Stanley K Komatsu *,, Alexander N Glazer *,ǁ
PMCID: PMC427251  PMID: 4202846

Abstract

A partial amino-acid sequence of Bacillus 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 of B. subtilis 168 flagellin with that derived from the flagellin of the serologically unrelated strain of B. 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 of Salmonella and Proteus with that on B. subtilis indicates homology between these proteins.

Keywords: Salmonella, Proteus, cyanogen bromide cleavage, tryptic digestion

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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