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. Author manuscript; available in PMC: 2018 Sep 4.
Published in final edited form as: Structure. 2016 Nov 23;25(1):203–211. doi: 10.1016/j.str.2016.10.010

Figure 2. BID Domain Arrangements and Subclasses in Beps and Relaxases.

Figure 2.

(A) The BID domain architecture as seen in two relaxases (TraA from Agrobacterium fabrum and Riorf112 from Agrobacterium rhizogenes), a VbhT homolog (VbhT from Bartonella schoenbuchensis), and representative B. henselae Beps, with vertical black lines indicating Tyr phosphorylation motifs and +++ the positively charged C terminus. MobA, mobilization proteins of the MobA/MobL family; AAA_30, ATPases associated with diverse cellular activities (AAA) domain; FIC, filamentation induced by cAMP domain; OB, oligonucleotide/oligosaccharide binding fold.

(B) Simplified neighbor-joining distance-based tree representation of the multiple sequence alignment of the BID domains from Beps and relaxases. The branches corresponding to Bep_tBIDx (ancestral) are colored in pink, Bep_tBIDx (derived) in blue, and Bep_BIDx in green (Engel et al., 2011). The relaxase tBID1 domains are colored in yellow, tBID2 in brown, and the BID1 in red. See Figure S3 for the full high-resolution tree shown here with species names and UniProt IDs.

(C) Classification scheme of BID domains developed in this study.

See also Figures S3 and S4.