Ditte Hededam Welner

Conflict of Interest The authors declare no conflict of interest. Data Availability Statement The data that support the findings of this study are available from the corresponding author upon reasonable request. Supporting Information Filename Description cbic70172-sup-0001-SuppData-S1.pdf1 MB Supplementary Material References 1, , , , Sci. Adv. 2016, 2, e1501623. 2, , , , , , , Dyes Pigm. 2022, 207, 110675. 3, , , , , , Isr. J. Chem. 2012, 52, 540. 4, , Ber. Dtsch. Chem. Ges. 1882, 15, 2856.

Filamentation induced by cAMP (Fic) domain proteins have been shown to catalyze the transfer of the AMP moiety from ATP onto a protein target. This type of post-translational modification was recently shown to play a crucial role in pathogenicity mediated by two bacterial virulence factors. Herein we characterize a novel Fic domain protein that we identified from the human pathogen Clostridium difficile.

Fic domain proteins have been shown to catalyze the transfer of the AMP moiety from ATP onto a protein target. This type of post-translational modification was recently shown to play a crucial role in pathogenicity mediated by two bacterial virulence factors. Herein we characterize a novel Fic domain protein that we identified from the human pathogen, Clostridium difficile.