Research graph
References from The <i>Shewanella oneidensis</i> Fic enzyme <scp>SoFic</scp> targets the switch‐I region of <scp>EF</scp> ‐Tu for <scp>AMPylation</scp>. Local targets link to admitted publications; unresolved targets remain external evidence.
Involvement of cyclic AMP and its receptor protein in filamentation of an Escherichia coli fic mutant
10.1128/jb.151.2.807-812.1982 · 1982 · External reference
Fido, a novel AMPylation domain common to fic, doc, and AvrB
10.1371/journal.pone.0005818 · 2009 · External reference
Biological diversity and molecular plasticity of FIC domain proteins
10.1146/annurev-micro-102215-095245 · 2016 · External reference
Revisiting AMPylation through the lens of fic enzymes
10.1016/j.tim.2021.08.003 · 2021 · External reference
FICD acts bifunctionally to AMPylate and de‐AMPylate the endoplasmic reticulum chaperone BiP
10.1038/nsmb.3337 · 2017 · External reference
A Ca(2+)‐regulated deAMPylation switch in human and bacterial FIC proteins
10.1038/s41467-019-09023-1 · 2019 · External reference
The DNA‐binding induced (de)AMPylation activity of a Coxiella burnetii fic enzyme targets histone H3
10.1038/s42003-023-05494-7 · 2023 · External reference
A Xanthomonas uridine 5′‐monophosphate transferase inhibits plant immune kinases
10.1038/nature10962 · 2012 · External reference
Pseudomonas effector AvrB is a glycosyltransferase that rhamnosylates plant guardee protein RIN4
10.1126/sciadv.add5108 · 2024 · External reference
Modulation of Rab GTPase function by a protein phosphocholine transferase
10.1038/nature10335 · 2011 · External reference
The fic protein doc uses an inverted substrate to phosphorylate and inactivate EF‐Tu
10.1038/nchembio.1364 · 2013 · External reference
AMPylation matches BiP activity to client protein load in the endoplasmic reticulum
10.7554/elife.12621 · 2015 · External reference
Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation
10.1074/jbc.m805654200 · 2008 · External reference
Plasmid addiction genes of bacteriophage P1: doc, which causes cell death on curing of prophage, and phd, which prevents host death when prophage is retained
10.1006/jmbi.1993.1521 · 1993 · External reference
A secreted effector with a dual role as a toxin and as a transcriptional factor
10.1038/s41467-022-35522-9 · 2022 · External reference
The fic domain: regulation of cell signaling by Adenylylation
10.1016/j.molcel.2009.03.008 · 2009 · External reference
AMPylation of rho GTPases by vibrio VopS disrupts effector binding and downstream signaling
10.1126/science.1166382 · 2009 · External reference
AMPylation of small GTPases by fic enzymes
10.1002/1873-3468.14516 · 2023 · External reference
Conformational control of small GTPases by AMPylation
10.1073/pnas.1917549117 · 2020 · External reference
Phosphorylation decelerates conformational dynamics in bacterial translation elongation factors
10.1126/sciadv.aap9714 · 2018 · External reference
Adenylylation control by intra‐ or intermolecular active‐site obstruction in fic proteins
10.1038/nature10729 · 2012 · External reference
Kinetic and structural insights into the mechanism of AMPylation by VopS fic domain
10.1074/jbc.m110.114884 · 2010 · External reference
Structural basis of fic‐mediated adenylylation
10.1038/nsmb.1867 · 2010 · External reference
Conserved inhibitory mechanism and competent ATP binding mode for Adenylyltransferases with fic fold
10.1371/journal.pone.0064901 · 2013 · External reference
Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD
10.1038/s41467-021-25076-7 · 2021 · External reference
An oligomeric state‐dependent switch in the ER enzyme FICD regulates AMPylation and deAMPylation of BiP
10.15252/embj.2019102177 · 2019 · External reference
Fic‐mediated deAMPylation is not dependent on homodimerization and rescues toxic AMPylation in flies
10.1074/jbc.m117.799296 · 2017 · External reference
Intrinsic regulation of FIC‐domain AMP‐transferases by oligomerization and automodification
10.1073/pnas.1516930113 · 2016 · External reference
Crystal structure of the fic (filamentation induced by cAMP) family protein SO4266 (gi|24375750) from Shewanella oneidensis MR‐1 at 1.6 a resolution
10.1002/prot.22338 · 2009 · External reference
Polyphasic taxonomy of the genus Shewanella and description of Shewanella oneidensis sp. nov
10.1099/00207713-49-2-705 · 1999 · External reference
Genome sequence of the dissimilatory metal ion‐reducing bacterium Shewanella oneidensis
10.1038/nbt749 · 2002 · External reference
Electroactive bacteria—molecular mechanisms and genetic tools
10.1007/s00253-014-6005-z · 2014 · External reference
Structural insights into the regulatory mechanisms of the toxic activity of Sofic in anti‐phage defense systems
10.3390/ijms26136074 · 2025 · External reference
The EMBL‐EBI job dispatcher sequence analysis tools framework in 2024
10.1093/nar/gkae241 · 2024 · External reference
InterPro: the protein sequence classification resource in 2025
10.1093/nar/gkae1082 · 2025 · External reference
The Pfam protein families database: embracing AI/ML
10.1093/nar/gkae997 · 2025 · External reference
Skylign: a tool for creating informative, interactive logos representing sequence alignments and profile hidden Markov models
10.1186/1471-2105-15-7 · 2014 · External reference
One‐step sequence‐ and ligation‐independent cloning as a rapid and versatile cloning method for functional genomics studies
10.1128/aem.00844-12 · 2012 · External reference
In‐gel digestion for mass spectrometric characterization of proteins and proteomes
10.1038/nprot.2006.468 · 2006 · External reference
The PRIDE database at 20 years: 2025 update
10.1093/nar/gkae1011 · 2025 · External reference
The functional dynamics of FicD's TPR domain are modulated by the interaction with ATP and BiP
10.1073/pnas.2500079122 · 2025 · External reference
10.1385/1-59259-890-0:571
10.1385/1-59259-890-0:571 · 2005 · External reference
eSPC: an online data‐analysis platform for molecular biophysics
10.1107/s2059798321008998 · 2021 · External reference
In‐depth interrogation of protein thermal unfolding data with MoltenProt
10.1002/pro.3986 · 2021 · External reference
NIH image to ImageJ: 25 years of image analysis
10.1038/nmeth.2089 · 2012 · External reference
Monoclonal anti‐AMP antibodies are sensitive and valuable tools for detecting patterns of AMPylation
10.1016/j.isci.2020.101800 · 2020 · External reference
Kinetic mechanism of elongation factor Ts‐catalyzed nucleotide exchange in elongation factor Tu
10.1021/bi015712w · 2002 · External reference
ColabFold: making protein folding accessible to all
10.1038/s41592-022-01488-1 · 2022 · External reference
Protein complexes in cells by AI‐assisted structural proteomics
10.15252/msb.202311544 · 2023 · External reference
XDS
10.1107/s0907444909047337 · 2010 · External reference
How good are my data and what is the resolution?
10.1107/s0907444913000061 · 2013 · External reference
Data processing and analysis with the autoPROC toolbox
10.1107/s0907444911007773 · 2011 · External reference
Phaser crystallographic software
10.1107/s0021889807021206 · 2007 · External reference
Features and development of Coot
10.1107/s0907444910007493 · 2010 · External reference
PHENIX: a comprehensive python‐based system for macromolecular structure solution
10.1107/s0907444909052925 · 2010 · External reference
MolProbity: all‐atom structure validation for macromolecular crystallography
10.1107/s0907444909042073 · 2010 · External reference
Implementing an X‐ray validation pipeline for the protein data Bank
10.1107/s0907444911050359 · 2012 · External reference
Legionella effector AnkX displaces the switch II region for Rab1b phosphocholination
10.1126/sciadv.aaz8041 · 2020 · External reference
Highly accurate protein structure prediction with AlphaFold
10.1038/s41586-021-03819-2 · 2021 · External reference
AlphaFold protein structure database and 3D‐beacons: new data and capabilities
10.1016/j.jmb.2025.168967 · 2025 · External reference
Universal and confident phosphorylation site localization using phosphoRS
10.1021/pr200611n · 2011 · External reference
The busiest of all ribosomal assistants: elongation factor Tu
10.1021/bi300077s · 2012 · External reference
Enzymes involved in AMPylation and deAMPylation
10.1021/acs.chemrev.7b00145 · 2018 · External reference
Crystal structure of intact elongation factor EF‐Tu from Escherichia coli in GDP conformation at 2.05 a resolution
10.1006/jmbi.1998.2387 · 1999 · External reference
The crystal structure of elongation factor EF‐Tu from Thermus aquaticus in the GTP conformation
10.1016/0969-2126(93)90007-4 · 1993 · External reference
The Caenorhabditis elegans protein FIC‐1 is an AMPylase that covalently modifies heat‐shock 70 family proteins, translation elongation factors and histones
10.1371/journal.pgen.1006023 · 2016 · External reference
Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD
10.1038/s41467-021-22596-0 · 2021 · External reference
Content of elongation factor Tu in Escherichia coli
10.1073/pnas.72.12.4780 · 1975 · External reference
The diverse functional roles of elongation factor Tu (EF‐Tu) in microbial pathogenesis
10.3389/fmicb.2019.02351 · 2019 · External reference
Translational regulation by modifications of the elongation factor Tu
10.1007/bf02816232 · 1999 · External reference
Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial ser/Thr/Tyr phosphorylation
10.1074/mcp.m700311-mcp200 · 2008 · External reference
Prokaryotic elongation factor Tu is phosphorylated in vivo
10.1016/s0021-9258(18)54193-4 · 1993 · External reference
Doc toxin is a kinase that inactivates elongation factor Tu
10.1074/jbc.m113.544429 · 2014 · External reference
Protein synthesis during cellular quiescence is inhibited by phosphorylation of a translational elongation factor
2015 · External reference
An alpha to beta conformational switch in EF‐Tu
10.1016/s0969-2126(96)00123-2 · 1996 · External reference
Structure and function of fic proteins
10.1038/nrmicro3520 · 2015 · External reference
AMPylation of small GTPases by fic enzymes
10.1002/1873-3468.14516 · ExternalCitation · doi-reference
In‐depth interrogation of protein thermal unfolding data with MoltenProt
10.1002/pro.3986 · ExternalCitation · doi-reference
Crystal structure of the fic (filamentation induced by cAMP) family protein SO4266 (gi|24375750) from Shewanella oneidensis MR‐1 at 1.6 a resolution
10.1002/prot.22338 · ExternalCitation · doi-reference
Plasmid addiction genes of bacteriophage P1: doc, which causes cell death on curing of prophage, and phd, which prevents host death when prophage is retained
10.1006/jmbi.1993.1521 · ExternalCitation · doi-reference
Crystal structure of intact elongation factor EF‐Tu from Escherichia coli in GDP conformation at 2.05 a resolution
10.1006/jmbi.1998.2387 · ExternalCitation · doi-reference
Translational regulation by modifications of the elongation factor Tu
10.1007/bf02816232 · ExternalCitation · doi-reference
Electroactive bacteria—molecular mechanisms and genetic tools
10.1007/s00253-014-6005-z · ExternalCitation · doi-reference
The crystal structure of elongation factor EF‐Tu from Thermus aquaticus in the GTP conformation
10.1016/0969-2126(93)90007-4 · ExternalCitation · doi-reference
Monoclonal anti‐AMP antibodies are sensitive and valuable tools for detecting patterns of AMPylation
10.1016/j.isci.2020.101800 · ExternalCitation · doi-reference
AlphaFold protein structure database and 3D‐beacons: new data and capabilities
10.1016/j.jmb.2025.168967 · ExternalCitation · doi-reference
The fic domain: regulation of cell signaling by Adenylylation
10.1016/j.molcel.2009.03.008 · ExternalCitation · doi-reference
Revisiting AMPylation through the lens of fic enzymes
10.1016/j.tim.2021.08.003 · ExternalCitation · doi-reference
Prokaryotic elongation factor Tu is phosphorylated in vivo
10.1016/s0021-9258(18)54193-4 · ExternalCitation · doi-reference
An alpha to beta conformational switch in EF‐Tu
10.1016/s0969-2126(96)00123-2 · ExternalCitation · doi-reference
Enzymes involved in AMPylation and deAMPylation
10.1021/acs.chemrev.7b00145 · ExternalCitation · doi-reference
Kinetic mechanism of elongation factor Ts‐catalyzed nucleotide exchange in elongation factor Tu
10.1021/bi015712w · ExternalCitation · doi-reference
The busiest of all ribosomal assistants: elongation factor Tu
10.1021/bi300077s · ExternalCitation · doi-reference
Universal and confident phosphorylation site localization using phosphoRS
10.1021/pr200611n · ExternalCitation · doi-reference
Modulation of Rab GTPase function by a protein phosphocholine transferase
10.1038/nature10335 · ExternalCitation · doi-reference
Adenylylation control by intra‐ or intermolecular active‐site obstruction in fic proteins
10.1038/nature10729 · ExternalCitation · doi-reference
A Xanthomonas uridine 5′‐monophosphate transferase inhibits plant immune kinases
10.1038/nature10962 · ExternalCitation · doi-reference
Genome sequence of the dissimilatory metal ion‐reducing bacterium Shewanella oneidensis
10.1038/nbt749 · ExternalCitation · doi-reference
The fic protein doc uses an inverted substrate to phosphorylate and inactivate EF‐Tu
10.1038/nchembio.1364 · ExternalCitation · doi-reference
NIH image to ImageJ: 25 years of image analysis
10.1038/nmeth.2089 · ExternalCitation · doi-reference
In‐gel digestion for mass spectrometric characterization of proteins and proteomes
10.1038/nprot.2006.468 · ExternalCitation · doi-reference
Structure and function of fic proteins
10.1038/nrmicro3520 · ExternalCitation · doi-reference
Structural basis of fic‐mediated adenylylation
10.1038/nsmb.1867 · ExternalCitation · doi-reference
FICD acts bifunctionally to AMPylate and de‐AMPylate the endoplasmic reticulum chaperone BiP
10.1038/nsmb.3337 · ExternalCitation · doi-reference
A Ca(2+)‐regulated deAMPylation switch in human and bacterial FIC proteins
10.1038/s41467-019-09023-1 · ExternalCitation · doi-reference
Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD
10.1038/s41467-021-22596-0 · ExternalCitation · doi-reference
Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD
10.1038/s41467-021-25076-7 · ExternalCitation · doi-reference
A secreted effector with a dual role as a toxin and as a transcriptional factor
10.1038/s41467-022-35522-9 · ExternalCitation · doi-reference
Highly accurate protein structure prediction with AlphaFold
10.1038/s41586-021-03819-2 · ExternalCitation · doi-reference
ColabFold: making protein folding accessible to all
10.1038/s41592-022-01488-1 · ExternalCitation · doi-reference
The DNA‐binding induced (de)AMPylation activity of a Coxiella burnetii fic enzyme targets histone H3
10.1038/s42003-023-05494-7 · ExternalCitation · doi-reference
Intrinsic regulation of FIC‐domain AMP‐transferases by oligomerization and automodification
10.1073/pnas.1516930113 · ExternalCitation · doi-reference
Conformational control of small GTPases by AMPylation
10.1073/pnas.1917549117 · ExternalCitation · doi-reference
The functional dynamics of FicD's TPR domain are modulated by the interaction with ATP and BiP
10.1073/pnas.2500079122 · ExternalCitation · doi-reference
Content of elongation factor Tu in Escherichia coli
10.1073/pnas.72.12.4780 · ExternalCitation · doi-reference
Kinetic and structural insights into the mechanism of AMPylation by VopS fic domain
10.1074/jbc.m110.114884 · ExternalCitation · doi-reference
Doc toxin is a kinase that inactivates elongation factor Tu
10.1074/jbc.m113.544429 · ExternalCitation · doi-reference
Fic‐mediated deAMPylation is not dependent on homodimerization and rescues toxic AMPylation in flies
10.1074/jbc.m117.799296 · ExternalCitation · doi-reference
Doc of prophage P1 is inhibited by its antitoxin partner Phd through fold complementation
10.1074/jbc.m805654200 · ExternalCitation · doi-reference
Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial ser/Thr/Tyr phosphorylation
10.1074/mcp.m700311-mcp200 · ExternalCitation · doi-reference
The PRIDE database at 20 years: 2025 update
10.1093/nar/gkae1011 · ExternalCitation · doi-reference
InterPro: the protein sequence classification resource in 2025
10.1093/nar/gkae1082 · ExternalCitation · doi-reference
The EMBL‐EBI job dispatcher sequence analysis tools framework in 2024
10.1093/nar/gkae241 · ExternalCitation · doi-reference
The Pfam protein families database: embracing AI/ML
10.1093/nar/gkae997 · ExternalCitation · doi-reference
Polyphasic taxonomy of the genus Shewanella and description of Shewanella oneidensis sp. nov
10.1099/00207713-49-2-705 · ExternalCitation · doi-reference
Phaser crystallographic software
10.1107/s0021889807021206 · ExternalCitation · doi-reference
MolProbity: all‐atom structure validation for macromolecular crystallography
10.1107/s0907444909042073 · ExternalCitation · doi-reference
XDS
10.1107/s0907444909047337 · ExternalCitation · doi-reference
PHENIX: a comprehensive python‐based system for macromolecular structure solution
10.1107/s0907444909052925 · ExternalCitation · doi-reference
Features and development of Coot
10.1107/s0907444910007493 · ExternalCitation · doi-reference
Data processing and analysis with the autoPROC toolbox
10.1107/s0907444911007773 · ExternalCitation · doi-reference
Implementing an X‐ray validation pipeline for the protein data Bank
10.1107/s0907444911050359 · ExternalCitation · doi-reference
How good are my data and what is the resolution?
10.1107/s0907444913000061 · ExternalCitation · doi-reference
eSPC: an online data‐analysis platform for molecular biophysics
10.1107/s2059798321008998 · ExternalCitation · doi-reference
Phosphorylation decelerates conformational dynamics in bacterial translation elongation factors
10.1126/sciadv.aap9714 · ExternalCitation · doi-reference
Legionella effector AnkX displaces the switch II region for Rab1b phosphocholination
10.1126/sciadv.aaz8041 · ExternalCitation · doi-reference
Pseudomonas effector AvrB is a glycosyltransferase that rhamnosylates plant guardee protein RIN4
10.1126/sciadv.add5108 · ExternalCitation · doi-reference
AMPylation of rho GTPases by vibrio VopS disrupts effector binding and downstream signaling
10.1126/science.1166382 · ExternalCitation · doi-reference
One‐step sequence‐ and ligation‐independent cloning as a rapid and versatile cloning method for functional genomics studies
10.1128/aem.00844-12 · ExternalCitation · doi-reference
Involvement of cyclic AMP and its receptor protein in filamentation of an Escherichia coli fic mutant
10.1128/jb.151.2.807-812.1982 · ExternalCitation · doi-reference
Biological diversity and molecular plasticity of FIC domain proteins
10.1146/annurev-micro-102215-095245 · ExternalCitation · doi-reference
Skylign: a tool for creating informative, interactive logos representing sequence alignments and profile hidden Markov models
10.1186/1471-2105-15-7 · ExternalCitation · doi-reference
The Caenorhabditis elegans protein FIC‐1 is an AMPylase that covalently modifies heat‐shock 70 family proteins, translation elongation factors and histones
10.1371/journal.pgen.1006023 · ExternalCitation · doi-reference
Fido, a novel AMPylation domain common to fic, doc, and AvrB
10.1371/journal.pone.0005818 · ExternalCitation · doi-reference
Conserved inhibitory mechanism and competent ATP binding mode for Adenylyltransferases with fic fold
10.1371/journal.pone.0064901 · ExternalCitation · doi-reference
10.1385/1-59259-890-0:571
10.1385/1-59259-890-0:571 · ExternalCitation · doi-reference
An oligomeric state‐dependent switch in the ER enzyme FICD regulates AMPylation and deAMPylation of BiP
10.15252/embj.2019102177 · ExternalCitation · doi-reference
Protein complexes in cells by AI‐assisted structural proteomics
10.15252/msb.202311544 · ExternalCitation · doi-reference
The diverse functional roles of elongation factor Tu (EF‐Tu) in microbial pathogenesis
10.3389/fmicb.2019.02351 · ExternalCitation · doi-reference
Structural insights into the regulatory mechanisms of the toxic activity of Sofic in anti‐phage defense systems
10.3390/ijms26136074 · ExternalCitation · doi-reference
AMPylation matches BiP activity to client protein load in the endoplasmic reticulum
10.7554/elife.12621 · ExternalCitation · doi-reference
