Molecular Cloning and Bioinformatics Analysis of T3SS Inner Membrane Ring HrpQ from Vibrio harveyi
1 College of Fishery, Guangdong Ocean University, Zhanjiang 524088, China
2 Guangdong Provincial Key Laboratory of Pathogenic Biology and Epidemiology for Aquatic Animals, Zhanjiang, 524088, China
3 Key Laboratory of Control for Diseases of Aquatic Animals of Guangdong Higher Education Institutes, Zhanjiang, 524088, China
Genomics and Applied Biology, 2018, Vol. 9, No. 7 doi: 10.5376/gab.2018.09.0007
Received: 15 Aug., 2018 Accepted: 23 Sep., 2018 Published: 10 Sep., 2018
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Preferred citation for this article:
Kuebutornye F.K.A., Liao J.M., Pang H.Y., Lu Y.S., Ayiku S., and Sakyi M.E., 2018, Molecular cloning and bioinformatics analysis of T3SS inner membrane ring HrpQ from Vibrio harveyi, Genomics and Applied Biology, 9(7): 40-47 (doi: 10.5376/gab.2018.09.0007)
In this study, Vibrio harveyi strain HY99 was isolated from a diseased Epinephelus coioides. A full-length HrpQ gene of the bacteria was cloned and the amino acid sequence analyzed. The length of HrpQ gene sequence was 1,302 bp and coded 433 Amino acids. HrpQ relative molecular weight of theoretical prediction and isoelectric point were 48.002 kDa and 5.08 respectively. This protein was hydrophilic and there was one transmembrane region. There were three N-glycosylation sites. Structural analysis showed that the protein belonged to the FHA, Yop-YscD ppl superfamily. Secondary structure was composed of 31.41% α-helices, 21.71% extension chains, 7.16% beta turns and 39.72% random curls. The 3D structure of HrpQ protein was predicted to be a monomer similar to the 3D structure of the YscD putative type III secretion protein confirming that HrpQ is a T3SS protein and can be activated in vivo. This study provides a theoretical basis for further study on the function of HrpQ protein.
Type III secretion system; Vibrio harveyi; HrpQ gene; Bioinformatics analysis
Genomics and Applied Biology
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