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DprA winged helix domain
This winged helix domain is found in the DprA protein [1]. [1]. 25138221. Roles of Bacillus subtilis DprA and SsbA in RecA-mediated genetic recombination. Yadav T, Carrasco B, Serrano E, Alonso JC;. J Biol Chem. 2014;289:27640-27652. (from Pfam)
DNA-processing protein DprA
The SMF family, of DNA processing chain A, dprA, are a group of bacterial proteins. In H. pylori, dprA is required for natural chromosomal and plasmid transformation [1]. It has now been shown that DprA is found to bind cooperatively to single-stranded DNA (ssDNA) and to interact with RecA. In the process, DprA-RecA-ssDNA filaments are produced and these filaments catalyse the homology-dependent formation of joint molecules. While the E.coli SSB protein limits access of RecA to ssDNA, DprA alleviates this barrier. It is proposed that DprA is a new member of the recombination-mediator protein family, dedicated to natural bacterial transformation [2]. [1]. 10640603. The dprA gene is required for natural transformation of Helicobacter pylori. Smeets LC, Bijlsma JJ, Kuipers EJ, Vandenbroucke-Grauls CM, Kusters JG;. FEMS Immunol Med Microbiol 2000;27:99-102. [2]. 17803906. A key presynaptic role in transformation for a widespread bacterial protein: DprA conveys incoming ssDNA to RecA. Mortier-Barriere I, Velten M, Dupaigne P, Mirouze N, Pietrement O, McGovern S, Fichant G, Martin B, Noirot P, Le Cam E, Polard P, Claverys JP;. Cell. 2007;130:824-836. (from Pfam)
DNA-processing protein DprA protects incoming foreign DNA and is an accessory factor for RecA-mediated DNA strand exchange
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