In silico Analysis of GGDEF Domain Proteins Functioning Differently in Xanthomonas campestris
1. State Key Laboratory of Non-food Biomass Enzyme Technology, National Engineering Research Center for Non-food Biorefinery, Guangxi Key Laboratory of Biorefinery, Guangxi Academy of Sciences, Nanning, 530007, P.R. China
2. Laboratory of Ministry of Education for Microbial and Plant Genetic Engineering, College of Life Science and Technology, Guangxi University, Nanning, 530004, P.R. China
Molecular Pathogens, 2012, Vol. 3, No. 1 doi: 10.5376/mp.2012.03.0001
Received: 11 Dec., 2011 Accepted: 17 Jan., 2012 Published: 19 Jan., 2012
© 2012 BioPublisher Publishing Platform
This article was first published in Genomics and Applied Biology in Chinese, and here was authorized to translate and publish the paper in English under the terms of Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Preferred citation for this article:
Zhang et al., 2012, In silico Analysis of GGDEF Domain Proteins Functioning Differently in Xanthomonas campestris, Molecular Pathogens, Vol.3, No.1 1-5 (doi: 10.5376/mp.2012.03.0001)
It has been reported that GGDEF domain proteins, containing five conserve amino acid residues with two glycines (G), one aspartic acid (D), one glutamic acid (E), and one phenylalanine (F) respectively, played key roles in the essential cell process of signal transduction, growth and pathogenicity. There are 32 GGDEF domain proteins were predicted in Xanthomonas campestris pv. campestris str. 8004 (Xcc 8004). And several of them were involved in the different cell processes of pathogenicity, production of extracellular enzyme, formation of biofilm and motility according to the experimental evidence. In this work, we analyzed the GGDEF domain proteins functioning differently in Xcc using bioinformatics web services, and focused on the analysis of the domain architectures. The results revealed that the overall domain architectures of these proteins were almost different except the PAS_4-GGDEF-EAL, which distributed in the proteins associated with virulence. According to the local comparison among the proteinic structures, the common domain architectures were found in the proteins involved in pathogenicity, including PAS_4-GGDEF and GGDEF-EAL. The PAS_4-PAS_4, PAS_4-GGDEF, and GGDEF-EAL in the proteins were involved in the production of endoglucanase in Xcc. The results of this research would provide some clues for inferring the function of proteins with GGDEF domain.
Xanthomonas campestris pv. campestris; GGDEF; Domain architecture; in silico analysis