{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T10:06:27Z","timestamp":1789725987444,"version":"4.0.1"},"reference-count":76,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T00:00:00Z","timestamp":1789689600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T00:00:00Z","timestamp":1789689600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["201302640"],"award-info":[{"award-number":["201302640"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["247377969"],"award-info":[{"award-number":["247377969"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["453548970"],"award-info":[{"award-number":["453548970"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["FEBS Letters"],"abstract":"<jats:p>\n                    Fic enzymes mediate diverse post\u2010translational modifications, including adenosine monophosphate (AMP) transfer and removal, referred to as AMPylation and deAMPylation, respectively. We identified the prokaryotic translation elongation factor Tu (EF\u2010Tu) as an AMPylation target of the Fic enzyme SoFic. SoFic can constitutively reverse EF\u2010Tu modification via deAMPylation whereas AMPylation depends on SoFic homodimerization. The complex crystal structure between SoFic and EF\u2010Tu confirms a conserved target binding mode across evolutionarily distant Fic enzymes. AMPylation disrupts EF\u2010Tu's regulatory switch\u2010I region, causing translational inhibition. SoFic furthermore binds to its promoter DNA\n                    <jats:italic>in vitro<\/jats:italic>\n                    , suggesting a dual function as transcriptional and translational regulator in bacterial cells. Together, our structural and biochemical data provide valuable insights into the functional and regulatory diversity of Fic enzymes.\n                  <\/jats:p>","DOI":"10.1002\/1873-3468.70457","type":"journal-article","created":{"date-parts":[[2026,9,18]],"date-time":"2026-09-18T09:26:04Z","timestamp":1789723564000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["The\n                    <i>Shewanella oneidensis<\/i>\n                    Fic enzyme\n                    <scp>SoFic<\/scp>\n                    targets the switch\u2010I region of\n                    <scp>EF<\/scp>\n                    \u2010Tu for\n                    <scp>AMPylation<\/scp>"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6607-426X","authenticated-orcid":false,"given":"Svenja","family":"Runge","sequence":"first","affiliation":[{"name":"Institute of Biochemistry and Signal Transduction University Medical Centre Hamburg\u2010Eppendorf (UKE)  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vivian","family":"Pogenberg","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Signal Transduction University Medical Centre Hamburg\u2010Eppendorf (UKE)  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander","family":"Baumgart","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Signal Transduction University Medical Centre Hamburg\u2010Eppendorf (UKE)  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bente","family":"Siebels","sequence":"additional","affiliation":[{"name":"Section Mass Spectrometry and Proteomics, Center for Diagnostics University Medical Centre Hamburg\u2010Eppendorf (UKE)  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hartmut","family":"Schl\u00fcter","sequence":"additional","affiliation":[{"name":"Section Mass Spectrometry and Proteomics, Center for Diagnostics University Medical Centre Hamburg\u2010Eppendorf (UKE)  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Hecht\u2010Bucher","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Signal Transduction University Medical Centre Hamburg\u2010Eppendorf (UKE)  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4249-5617","authenticated-orcid":false,"given":"Aymelt","family":"Itzen","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Signal Transduction University Medical Centre Hamburg\u2010Eppendorf (UKE)  Germany"},{"name":"Centre of Structural Systems Biology (CSSB), Institute of Biochemistry and Signal Transduction University Medical Centre Hamburg\u2010Eppendorf (UKE)  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,9,18]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1128\/jb.151.2.807-812.1982","article-title":"Involvement of cyclic AMP and its receptor protein in filamentation of an Escherichia coli fic mutant","volume":"151","author":"Utsumi R","year":"1982","journal-title":"J Bacteriol"},{"key":"e_1_2_9_3_1","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0005818","article-title":"Fido, a novel AMPylation domain common to fic, doc, and AvrB","volume":"4","author":"Kinch LN","year":"2009","journal-title":"PLoS One"},{"key":"e_1_2_9_4_1","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1146\/annurev-micro-102215-095245","article-title":"Biological diversity and molecular plasticity of FIC domain proteins","volume":"70","author":"Harms A","year":"2016","journal-title":"Ann Rev 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activity of a Coxiella burnetii fic enzyme targets histone H3","volume":"6","author":"H\u00f6pfner D","year":"2023","journal-title":"Commun Biol"},{"key":"e_1_2_9_9_1","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1038\/nature10962","article-title":"A Xanthomonas uridine 5\u2032\u2010monophosphate transferase inhibits plant immune kinases","volume":"485","author":"Feng F","year":"2012","journal-title":"Nature"},{"key":"e_1_2_9_10_1","doi-asserted-by":"crossref","first-page":"eadd5108","DOI":"10.1126\/sciadv.add5108","article-title":"Pseudomonas effector AvrB is a glycosyltransferase that rhamnosylates plant guardee protein RIN4","volume":"10","author":"Peng W","year":"2024","journal-title":"Sci Adv"},{"key":"e_1_2_9_11_1","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/nature10335","article-title":"Modulation of Rab GTPase function by a protein phosphocholine transferase","volume":"477","author":"Mukherjee 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AJ","year":"2007","journal-title":"J Appl Crystallogr"},{"key":"e_1_2_9_55_1","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley P","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_2_9_56_1","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive python\u2010based system for macromolecular structure solution","volume":"66","author":"Adams PD","year":"2010","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_2_9_57_1","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all\u2010atom structure validation for macromolecular crystallography","volume":"66","author":"Chen VB","year":"2010","journal-title":"Acta Crystallogr D Biol 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