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Type II Toxin-Antitoxin Loci: The fic Family

  • Arnaud Goepfert
  • Alexander Harms
  • Tilman Schirmer
  • Christoph Dehio
Chapter

Abstract

FIC domain containing proteins (Fic proteins) are present in all domains of life but particularly widespread among prokaryotes. FIC domains with a fully conserved HxFx[D/E]GNGRxxR active site motif catalyze adenylylation (also known as AMPylation), the transfer of an adenosine 5′-monophosphate moiety onto target proteins. Adenylylation activity is tightly controlled by an inhibitory α-helix (α inh) that can either be part of the Fic protein (intramolecular inhibition) or encoded on a different polypeptide chain (intermolecular inhibition), the latter constituting a novel class of type II toxin-antitoxin (TA) modules represented by VbhT-VbhA of Bartonella schoenbuchensis and FicT-FicA of Escherichia coli. The helix α inh harbors a [S/T]xxxE[G/N] motif with the conserved glutamate partially obstructing the ATP-binding site and forcing ATP to bind in a catalytically incompetent conformation. Release of inhibition by removal of the antitoxin component or by mutation of the conserved glutamate in α inh converts Fic proteins into toxins that severely impair bacterial growth.

Keywords

Xanthomonas Campestris Active Site Motif Secretion Effector Protein Active Site Location Intermolecular Salt Bridge 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 2013

Authors and Affiliations

  • Arnaud Goepfert
    • 1
    • 2
  • Alexander Harms
    • 1
  • Tilman Schirmer
    • 2
  • Christoph Dehio
    • 1
  1. 1.Focal Area Infection Biology, BiozentrumUniversity of BaselBaselSwitzerland
  2. 2.Focal Area Structural Biology and Biophysics, BiozentrumUniversity of BaselBaselSwitzerland

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