A strain-variable bacteriocin in Bacillus anthracis and Bacillus cereus with repeated Cys-Xaa-Xaa motifs.
Bacteriocins are peptide antibiotics from ribosomally translated precursors, produced by bacteria often through extensive post-translational modification. Minimal sequence conservation, short gene lengths, and low complexity sequence can hinder bacteriocin identification, even during gene calling, so they are often discovered by proximity to accessory genes encoding maturation, immunity, and export functions. This work reports a new subfamily of putative thiazole-containing heterocyclic bacteriocins. It appears universal in all strains of Bacillus anthracis and B. cereus, but has gone unrecognized because it is always encoded far from its maturation protein operon. Patterns of insertions and deletions among twenty-four variants suggest a repeating functional unit of Cys-Xaa-Xaa.
Haft
Daniel H
DH
The J. Craig Venter Institute, 9704 Medical Center Drive, Rockville, MD 20850, USA. haft@jcvi.org
D020816:Amino Acid Motifs; D001408:Bacillus anthracis / Q000737:chemistry* / Q000145:classification*; D001409:Bacillus cereus / Q000737:chemistry* / Q000145:classification*; D001430:Bacteriocins / Q000737:chemistry*; D003545:Cysteine / Q000737:chemistry; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D013045:Species Specificity
D001430:Bacteriocins; D003545:Cysteine