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The core genetic regulatory components of the GSR are required for<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. abortus<\/jats:named-content>survival under nonoptimal growth conditions<jats:italic>in vitro<\/jats:italic>and for maintenance of chronic infection in an<jats:italic>in vivo<\/jats:italic>mouse model. The functions of the majority of the genes in the GSR transcriptional regulon remain undefined.<jats:italic>bab1_1070<\/jats:italic>is among the most highly regulated genes in this regulon: its transcription is activated 20- to 30-fold by the GSR system under oxidative conditions<jats:italic>in vitro<\/jats:italic>. We have solved crystal structures of Bab1_1070 and demonstrate that it forms a homotetrameric complex that resembles those of WrbA-type NADH:quinone oxidoreductases, which are members of the flavodoxin protein family. However,<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. abortus<\/jats:named-content><jats:underline>W<\/jats:underline>rbA-<jats:underline>r<\/jats:underline>elated<jats:underline>p<\/jats:underline>rotein (WrpA) does not bind flavin cofactors with a high affinity and does not function as an NADH:quinone oxidoreductase<jats:italic>in vitro<\/jats:italic>. Soaking crystals with flavin mononucleotide (FMN) revealed a likely low-affinity binding site adjacent to the canonical WrbA flavin binding site. Deletion of<jats:italic>wrpA<\/jats:italic>(\u0394<jats:italic>wrpA<\/jats:italic>) does not compromise cell survival under acute oxidative stress<jats:italic>in vitro<\/jats:italic>or attenuate infection in cell-based or mouse models. However, a \u0394<jats:italic>wrpA<\/jats:italic>strain does elicit increased splenomegaly in a mouse model, suggesting that WrpA modulates<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. abortus<\/jats:named-content>interaction with its mammalian host. Despite high structural homology with canonical WrbA proteins, we propose that<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. abortus<\/jats:named-content>WrpA represents a functionally distinct member of the diverse flavodoxin family.<\/jats:p><jats:p><jats:bold>IMPORTANCE<\/jats:bold><jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Brucella abortus<\/jats:named-content>is an etiological agent of brucellosis, which is among the most common zoonotic diseases worldwide. The general stress response (GSR) regulatory system of<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">B. abortus<\/jats:named-content>controls the transcription of approximately 100 genes and is required for maintenance of chronic infection in a murine model; the majority of GSR-regulated genes remain uncharacterized. We present<jats:italic>in vitro<\/jats:italic>and<jats:italic>in vivo<\/jats:italic>functional and structural analyses of WrpA, whose expression is strongly induced by GSR under oxidative conditions. Though WrpA is structurally related to NADH:quinone oxidoreductases, it does not bind redox cofactors in solution, nor does it exhibit oxidoreductase activity<jats:italic>in vitro<\/jats:italic>. However, WrpA does affect spleen inflammation in a murine infection model. Our data provide evidence that WrpA forms a new functional class of WrbA\/flavodoxin family proteins.<\/jats:p>","DOI":"10.1128\/jb.00982-15","type":"journal-article","created":{"date-parts":[[2016,2,9]],"date-time":"2016-02-09T04:37:03Z","timestamp":1454992623000},"page":"1281-1293","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":16,"title":["WrpA Is an Atypical Flavodoxin Family Protein under Regulatory Control of the Brucella abortus General Stress Response System"],"prefix":"10.1128","volume":"198","author":[{"given":"Julien","family":"Herrou","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA"},{"name":"Howard Taylor Ricketts Laboratory, University of Chicago, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel M.","family":"Czy\u017c","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA"},{"name":"Howard Taylor Ricketts Laboratory, University of Chicago, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jonathan W.","family":"Willett","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA"},{"name":"Howard Taylor Ricketts Laboratory, University of Chicago, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hye-Sook","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA"},{"name":"Howard Taylor Ricketts Laboratory, University of Chicago, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gekleng","family":"Chhor","sequence":"additional","affiliation":[{"name":"Argonne National Laboratory, Argonne, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gyorgy","family":"Babnigg","sequence":"additional","affiliation":[{"name":"Argonne National Laboratory, Argonne, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Youngchang","family":"Kim","sequence":"additional","affiliation":[{"name":"Argonne National Laboratory, Argonne, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sean","family":"Crosson","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois, USA"},{"name":"Howard Taylor Ricketts Laboratory, University of Chicago, Chicago, Illinois, USA"},{"name":"Department of Microbiology, University of Chicago, Chicago, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrmicro3032"},{"key":"e_1_3_3_3_2","first-page":"1","article-title":"Bacterial resistance mechanism against oxidative stress","volume":"2","author":"Mishra A","year":"2015","unstructured":"Mishra A, Mishra KP. 2015. 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