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Unlike externally flagellated bacteria, spirochetes possess a unique periplasmic flagellar structure called the collar. This spirochete\u2010specific novel component is linked to the flagellar basal body; however, nothing is known about the proteins encoding the collar or their function in any spirochete. To identify a collar protein and determine its function, we employed a comprehensive strategy that included genetic, biochemical, and microscopic analyses. We found that BB0286 (FlbB) is a novel flagellar motor protein, which is located around the flagellar basal body. Deletion of <jats:italic>bb0286<\/jats:italic> has a profound effect on collar formation, assembly of other flagellar structures, morphology, and motility of the spirochete. Orientation of the flagella toward the cell body is critical for determination of wild\u2010type spirochete's wave\u2010like morphology and motility. Here, we provide the first evidence that FlbB is a key determinant of normal orientation of the flagella and collar assembly.<\/jats:p>","DOI":"10.1111\/mmi.13463","type":"journal-article","created":{"date-parts":[[2016,7,15]],"date-time":"2016-07-15T09:56:32Z","timestamp":1468576592000},"page":"336-348","source":"Crossref","is-referenced-by-count":45,"title":["Spirochetes flagellar collar protein FlbB has astounding effects in orientation of periplasmic flagella, bacterial shape, motility, and assembly of motors in <i>Borrelia burgdorferi<\/i>"],"prefix":"10.1111","volume":"102","author":[{"given":"Ki Hwan","family":"Moon","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunology, Brody School of Medicine East Carolina University Greenville NC USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaowei","family":"Zhao","sequence":"additional","affiliation":[{"name":"Department of Pathology and Laboratory Medicine University of Texas Health 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