OPINION

Serine/threonine protein kinases of bacteria are potential targets for regulation of human microbiota composition

About authors

1 Laboratory of Bacterial Genetics, Vavilov Institute of General Genetics of RAS, Moscow

2 Department of Bioinformatics, Faculty of Biological and Medical Physics,
Moscow Institute of Physics and Technology (State University), Dolgoprudny

Correspondence should be addressed: Natalia Zakharevich
ul. Gubkina, d. 3, Moscow, Russia, 119991; ur.xednay@hciverahkaz

About paper

All authors' contribution to this work is equal: selection and analysis of literature, planning of the manuscript's structure, data interpretation, drafting of the manuscript, editing.

Received: 2017-03-28 Accepted: 2017-04-07 Published online: 2017-05-31
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Fig. 1. A simplified representation of the adenine-binding pocket showing the signature amino acid residues (Tyr94 is not shown). The first three residues belong to the glycine loop (residues 17–38). They form the “ceiling” of the adenine-binding pocket. The hinge sequence consists of residues 92–96 (Met92 is the gatekeeper), but residues 93 and 96 contribute to ligand binding only with their backbone atoms, therefore, they were excluded from consideration
Fig. 2. Groups of STPKs of gram-positive bacteria (Zakharevich et al., [19])
Fig. 3. This Venn diagram represents distribution of groups of serine/threonine protein kinases into three clusters. Roman numerals represent kinase groups according to our classification (Zakharevich et al., [19]). Groups XIV, XV, XVII, and XX are not included because: 1) the microorganisms belonging to these groups are neither pathogens nor symbionts of the human microbiota and 2) no similarities were detected between STPK signatures of these 4 groups and signatures of human protein kinases
The profile of STPKs from groups VII, X, XVIII, and XIX, characteristic for pathogens