Fig. 2

Structural comparisons of the Pmp and BspA protein family in different trichomonads. Schematic illustration of selected Pmp structures in different trichomonadida together with the prokaryotic model Chlamydia trachomatis (accession numbers: C. trachomatis, gi 34539119; T. vaginalis, TVAG_249300; P. hominis, PEHa011017; T. gallinae, TEGb004672; Tet. gallinarum, TRGa004464; T. tenax, TRTa003481). The Pmp family is characterized by multiple repeats of the FxxN and GGA[I/L/V] motifs located in the N-terminal region but compared to C. trachomatis the trichomonad proteins miss the C-terminal polymorphic middle and autotransporter domain. Instead they possess a conserved ATPITK motif as well as a transmembrane domain at their C-terminus. Selected members the BspA family of different trichomonadida compared to one of Tannerella forsythia (accession numbers: T. forsythia, gi 3005673; T. vaginalis, TVAG_240680; P. hominis, PEHa029834; T. gallinae, TEGb004448; Tri. batrachorum, TRBa028008; Tet. gallinarum, TRGa003876; T. tenax, TRTa008806). The BspA protein family is unified by several N-terminal copies of leucine-rich-repeat elements. In T. forsythia the BspA additionally possess a bacterial Ig-like domain (Big-domain) as well as a por secretion system both localized towards the C-terminus. In the trichomonads, those are replaced by a transmembrane domain in a proportion of BspA-like proteins