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Article

The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu.

Nature chemical biology - 1 Dec 2013

Castro-Roa Daniel, Garcia-Pino Abel, De Gieter Steven, van Nuland Nico A J, Loris Remy, Zenkin Nikolay

Abstract excerpt

Fic proteins are ubiquitous in all of the domains of life and have critical roles in multiple cellular processes through AMPylation of (transfer of AMP to) target proteins. Doc from the doc-phd toxin-antitoxin module is a member of the Fic family and inhibits bacterial translation by an unknown mechanism. Here we show that, in contrast to having AMPylating activity, Doc is a new type of kinase that inhibits...

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Share to Escherichia coli Proteins
Share to Gene Expression Regulation, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Guanosine Triphosphate

Share to Nucleotidyltransferases

Share to Peptide Elongation Factor Tu

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Identifiers

PMID: 24141193
DOI: 10.1038/nchembio.1364
PMCID: PMC3836179

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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