Figure 1

Amino acid motifs in the Bat proteins of L. biflexa . The vWF and TPR domains are conserved among Bat homologs and have been proposed to facilitate formation of a large Bat protein complex [4]. The vWF domains identified in Bat proteins contain metal ion-dependent adhesion sites (MIDAS) shown to bind metal ions [10] and the domain overall is thought to mediate protein-protein interactions [11]. The TPR domain of BatB consists of a repeated amino acid motif previously shown to form a tertiary scaffold structure for multiprotein complex formation (reviewed in [12]). These domains, along with the presence of multiple transmembrane helices and a signal sequence identified in BatD, suggest that the Bat proteins form a complex associated with either the inner or outer membrane of L. biflexa.