Sequence analyses of fimbriae subunit FimA proteins on genospecies 1 and 2 and with variant carbohydrate binding specificities-2

<p><b>Copyright information:</b></p><p>Taken from "Sequence analyses of fimbriae subunit FimA proteins on genospecies 1 and 2 and with variant carbohydrate binding specificities"</p><p>BMC Microbiology 2006;6():43-43.</p><p>Published online 10 May 2006</p><p>PMCID:PMC1473193.</p><p>Copyright © 2006 Drobni et al; licensee BioMed Central Ltd.</p>) sequence identity between FimA proteins. The low FimA amino acid (a.a.) sequence identity regions (unlined, double and triple lined white boxes) are species-specific due to a high strain-to-strain sequence identity for each species. High FimA sequence identity domains include the N-terminal signal peptide, pilin motif, proline-rich region, E box, and LPXTG motif (motifs are marked and the seven conserved proline-containing domains identified by Yeung and Cisar are numbered). The proline-containing domains 1 and 5 of FimA display only a conserved proline residue, in contrast to FimP, in which the entire seven proline-containing domains are conserved. The FimA proteins from genospecies 1 and 2 and contains 32, 33 and 32 amino acid signal peptides and 534, 535 and 535 amino acid proteins, respectively. Alignment of the pilin, E-box and LPXTG motifs present in FimA from different strains. Postulated key determinants are in bold [29, 39]