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Structural and functional characterization of microcin C
resistance peptidase MccF from Bacillus anthracis  Journal of
molecular biology  2012;420(0):366-383. Microcin C (McC) is
heptapeptide-adenylate antibiotic produced by Escherichia coli
strains carrying the mccABCDEF gene cluster encoding enzymes, in
addition to the heptapeptide structural gene mccA, necessary for
McC biosynthesis and self-immunity of the producing cell. The
heptapeptide facilitates McC transport into susceptible cells,
where it is processed releasing a non-hydrolyzable aminoacyl
adenylate that inhibits an essential aminoacyl-tRNA synthetase.
The self-immunity gene mccF encodes a specialized serine-
peptidase that cleaves an amide bond connecting the peptidyl or
aminoacyl moieties of, respectively, intact and processed McC
with the nucleotidyl moiety. Most mccF orthologs from organisms
other than E. coli are not link