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Figure 1 | BMC Microbiology

Figure 1

From: A systematic analysis of the in vitro and in vivo functions of the HD-GYP domain proteins of Vibrio cholerae

Figure 1

Domain architectures and sequence conservation of putative HD-GYP domain proteins of V. cholerae . (A) Predicted domains of the nine HD-GYP domain proteins encoded by V. cholerae. Shown are HD-GYP domains (blue), phosphoreceiver domains (red), HAMP domains (green), domains of unknown function (white) and putative transmembrane domains (black). The lengths of the proteins (number of amino acids) are indicated. (B) Alignment of V. cholerae HD-GYP domains. The HD-GYP domain amino acid sequences from V. cholerae, including the two tandem domains in VCA0681, were aligned to the HD-GYP domains of RpfG from X. campestris and Pm GH from Persephonella marina using Clustal Omega software. Highlighted are the HD and GYP motifs (yellow), identical amino acid residues (orange) and conserved amino acid residues (green). Asterisks indicate residues previously shown to be required for enzymatic activity of Pm GH [61].

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