Fig 1.
Summary of the DivIVA-like domain.
(A) Cartoon renders of the DivIVA N-terminal domain (2WUJ); color-coded to match panel C, are the residues of the conserved motif as well as the core residues of the two following heptad coiled coils. (B) Superimposition of DivIVA (2WUJ, white), GpsB (4UG3, gray) and Wag31 (6LFA, teal); RMSD of the superimposition to 2WUJ is 1.0 and 2.2 Angstrom respectively. (C) Alignment of the sequences for the structures shown in panel B to the consensus sequences (N = number of sequences) of representatives for the major groups of DivIVA homologs (see Methods); the conserved motif and the core residues of the two following heptad coiled coils are highlighted in colors, and the Quick2D α-helical prediction is shown as underlined characters. (D) Logo representation of the top scoring motif found by MEME in the set of 1816 DivIVA homologs obtained as described in the Methods.
Fig 2.
A broad survey of DivIVA-like proteins.
(A) Cluster map of sequences with a match to the conserved motif in DivIVA-like proteins (see Methods). Clustering was done in 2D until equilibrium at a BLAST P-value of 1E-10. Connections represent similarities up to a P-value of 1E–10. The three groups of clusters that feature a DivIVA-like domain are colored and labeled. Cartoon representation of the sequence features for representative sequences of Scy/FilP (B), DivIVA/GpsB (C), and PolyDIV groups (D).
Fig 3.
Examples of the topologies observed in the PolyDIV AlphaFold models.
Colored from N-terminus (blue) to C-terminus (red). (A) The PURPLE_3_monomer model shows its DivIVA-like domains interacting in a consecutive manner, first with second and third with fourth. (B) The PURPLE_3+DivIVA_monomer shows a non-consecutive DivIVA-like topology. (C) PURPLE_3_dimer shows a topology equivalent to that of (A), where the two chains do not interact via their DivIVA-like domains. (D) PURPLE_1_dimer shows a complex topology where one or more DivIVA-like domains interact with another DivIVA-like domain from another polypeptide chain. All sequences and models are provided in the S1 File.
Fig 4.
Evolutionary scenario for proteins containing the DivIVA-like domain.
The diversity of the DivIVA-like superfamily seems to have arisen mainly through events of duplication (intra- or intergenic) and coiled-coil repeat expansion. The deepest branching point in this tree is an orthologous split due to the separation between Firmicutes and Actinobacteria. All other branch points are due to paralogy.