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The bacterium\n                    <jats:named-content content-type=\"genus-species\">Serratia marcescens<\/jats:named-content>\n                    is part of the\n                    <jats:named-content content-type=\"genus-species\">Enterobacteriaceae<\/jats:named-content>\n                    family of eubacteria and produces a number of biologically active secondary metabolites. In this study, we screened for novel regulators of secondary metabolites synthesized by a clinical isolate of\n                    <jats:named-content content-type=\"genus-species\">S. marcescens<\/jats:named-content>\n                    and found mutations in a gene for an uncharacterized UmoB\/IgaA family member here named\n                    <jats:italic>gumB<\/jats:italic>\n                    . Mutation of\n                    <jats:italic>gumB<\/jats:italic>\n                    conferred a severe loss of the secondary metabolites prodigiosin and serratamolide. The\n                    <jats:italic>gumB<\/jats:italic>\n                    mutation conferred pleiotropic phenotypes, including altered biofilm formation, highly increased capsular polysaccharide production, and loss of swimming and swarming motility. These phenotypes corresponded to transcriptional changes in\n                    <jats:italic>fimA<\/jats:italic>\n                    ,\n                    <jats:italic>wecA<\/jats:italic>\n                    , and\n                    <jats:italic>flhD<\/jats:italic>\n                    . Unlike other UmoB\/IgaA family members,\n                    <jats:italic>gumB<\/jats:italic>\n                    was found to be not essential for growth in\n                    <jats:named-content content-type=\"genus-species\">S. marcescens<\/jats:named-content>\n                    , yet\n                    <jats:italic>igaA<\/jats:italic>\n                    from\n                    <jats:named-content content-type=\"genus-species\">Salmonella enterica<\/jats:named-content>\n                    ,\n                    <jats:italic>yrfF<\/jats:italic>\n                    from\n                    <jats:named-content content-type=\"genus-species\">Escherichia coli<\/jats:named-content>\n                    , and an uncharacterized predicted ortholog from\n                    <jats:named-content content-type=\"genus-species\">Klebsiella pneumoniae<\/jats:named-content>\n                    complemented the\n                    <jats:italic>gumB<\/jats:italic>\n                    mutant secondary metabolite defects, suggesting highly conserved function. These data support the idea that UmoB\/IgaA family proteins are functionally conserved and extend the known regulatory influence of UmoB\/IgaA family proteins to the control of competition-associated secondary metabolites and biofilm formation.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:bold>IMPORTANCE<\/jats:bold>\n                    IgaA\/UmoB family proteins are found in members of the\n                    <jats:named-content content-type=\"genus-species\">Enterobacteriaceae<\/jats:named-content>\n                    family of bacteria, which are of environmental and public health importance. IgaA\/UmoB family proteins are thought to be inner membrane proteins that report extracellular stresses to intracellular signaling pathways that respond to environmental challenge. This study introduces a new member of the IgaA\/UmoB family and demonstrates a high degree of functional similarity between IgaA\/UmoB family proteins. Moreover, this study extends the phenomena controlled by IgaA\/UmoB family proteins to include the biosynthesis of antimicrobial secondary metabolites.\n                  <\/jats:p>","DOI":"10.1128\/aem.02575-17","type":"journal-article","created":{"date-parts":[[2018,1,8]],"date-time":"2018-01-08T07:13:12Z","timestamp":1515395592000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":27,"title":["An IgaA\/UmoB Family Protein from Serratia marcescens Regulates Motility, Capsular Polysaccharide Biosynthesis, and Secondary Metabolite Production"],"prefix":"10.1128","volume":"84","author":[{"given":"Nicholas A.","family":"Stella","sequence":"first","affiliation":[{"name":"Charles T. 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