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. Author manuscript; available in PMC: 2012 Jan 12.
Published in final edited form as: Chem Rev. 2010 Dec 21;111(1):117–151. doi: 10.1021/cr100370n

Figure 8.

Figure 8

Alignments of cytoplasmic domains of HPKs. PHYRE310 was used to align the sequence of AgrC-I, HK853 from Thermotoga maritima, and EnvZ and PhoQ from E. coli. Residues that are highly conserved in HPK10's are highlighted in red and residues that are highly conserved in HK853, EnvZ and PhoQ are highlighted in yellow. AgrC-I residues highlighted in blue have a high propensity for coiled-coil formation, and AgrC-I residues highlighted in green are positions where mutations result in constitutive activity. EnvZ residues highlighted in green are positions where mutations eliminate phosphatase activity without altering autokinase activity. Underlined HK853 residues are within α-helices and boxed HK853 residue are within β-strands. The locations of the DHp subdomain and the X-region are indicated. Protein and bacteria names as well as specific residue numbering are indicated in the margins, and a residue count line is provided at the top of each panel.