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Figure 1 | BMC Microbiology

Figure 1

From: Structure-based discovery of inhibitors of the YycG histidine kinase: New chemical leads to combat Staphylococcus epidermidis infections

Figure 1

Domain analysis of the YycG/YycF TCS of S. epidermidis. (A) Domain analysis of the two-component system (TCS) YycG/YycF of S. epidermidis ATCC12228. The analysis was performed based on the SMART database and the descriptions of putative functions of domains were also from SMART. HAMP: dimerization; PAS: FAD, heme, and cinnamic acid binding; HisKA: Phosphoacceptor, dimerization; HATPase_c: ATP-binding, Phosphorylation of HisKA domain, REC: phosphoacceptor, Trans_reg_C: DNA binding. The columns represent the transmembrane segment predicted by the TMHMM2 program, and the arrows indicate the start and end sites of the YycG protein fragment – YycG', as described in EXPERIMENTAL PROCEDUES. (B) The sequence alignment of the HATPase_c domain of YycG in S. epidermidis and that of EnvZ in E. coli. The height of columns below the alignment represents the similarity between two proteins. "*" denotes identical residues between two sequences, ":" means similar residues, "." means a bit different, and blank means completely different. Schematic alignment diagram was made by the program ClustalX.

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