Amplification and Bioinformatics Analysis of vscN Gene from Vibrio alginolyticus

[Objectives] The paper was to clone and analyze bioinformatics of vscN gene from Vibrio alginolyticus. [Methods] A pair of specific primers was designed based on the vscN gene sequence of V. alginolyticus HY9901. The full length of vscN gene was amplified by PCR and bioinformatics analysis was performed. [Results] The vscN gene was 1 323 bp in total, encoding 440 amino acids, with the theoretical molecular weight of 47.86 kD and the theoretical pI value of 5.89. The online prediction showed that there was no signal peptide and no transmembrane region in VscN. The amino acid sequence had 10 N-myristoylation sites, 8 phosphorylation sites (2 protein kinase C phosphorylation sites, 6 casein kinase II phosphorylation sites), 1 amidation site, 11 microbody C-terminal target signal sites, 1 ATP/GTP binding site motif A (P ring), and 1 ATPase α and β subunit specific site. Homology analysis showed that the VscN protein of V. alginolyticus had high homology with that of V. antiquarius, with a similarity of 95.14%. Phylogenetic tree analysis showed that the VscN of V. alginolyticus was clustered into the same subgroup as that of V. diabolicus and V. antiquarius. Functional domain analysis of VscN protein showed that it had Pfam and AAA domains, and involved in the regulation of bacterial virulence. The three-dimensional structure model of VscN simulated by SWISS-MODEL software was similar to the structure of flagellate-specific ATPase FliH-FliI complex. [Conclusions] The results lay a foundation for further study on the regulatory mechanism of VscN protein on bacterial virulence.