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ProteomicsThe DNA-binding induced (de)AMPylation activity of a Coxiella burnetii Fic enzyme targets Histone H3
Intracellular bacterial pathogens such as Coxiella burnetii evade their host's immune response by secreting effector proteins that bind and modify host proteins, thereby reshaping cell signaling pathways that help establish a replication-friendly niche. Previous research has identified Filamentation...
ORGANISM(S): Homo sapiens (Human) Coxiella burnetii cb109 
2024-01-26 | PXD040330 | Pride
Ampylation Histone h3 Fic enzyme Dna-binding Coxiella burnetii 
ProteomicsStructural basis of chaperone regulation by a post-translational modification
The Hsp70 chaperone BiP is covalently modified with adenosine monophosphate (referred to as AMPylation) in order to adapt its activity to the fluctuating folding load within the endoplasmic reticulum. This modification is catalyzed by the only human representative of the family of filamentation indu...
ORGANISM(S): Homo sapiens (Human) 
2021-04-27 | PXD022869 | Pride
Hype Ampylation Hsp70 chaperone bip 
ProteomicsThe Shewanella oneidensis Fic enzyme SoFic targets theswitch-I region of EF-Tu for AMPylation
Fic enzymes mediate diverse post-translational modifications, including adeno-sine monophosphate (AMP) transfer and removal, referred to as AMPylationand deAMPylation, respectively. We identified the prokaryotic translationelongation factor Tu (EF-Tu) as an AMPylation target of the Fic enzymeSoFic. ...
ORGANISM(S): Escherichia coli 
2026-09-18 | PXD071331 | Pride
Structural regulation Ampylation Ef-tu Fic enzymes Deampylation 
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