Molecular Cloning and Bioinformatics Analysis of msrA Gene from Vibrio alginolyticus Strain HY9901.

[Objectives] This study was conducted to understand the structure and function of MsrA protein. [Methods] With Vibrio alginolyticus HY9901 as the object of study, primers were designed to amplify the full-length gene of msrA, and its bioinformatics analysis was carried out. [Results] The full length of msrA gene was 639 bp, encoding 212 amino acids, and its theoretical molecular weight was about 23 729.60 Da. The protein had a stable structure, and it was hydropho-bic overall. The structure of signal peptides at the N terminal of the amino acid sequence was predicted, and it was found that there was no signal peptide cleavage site and no transmembrane region. The amino acid sequence of MsrA contained multiple signal binding sites. Protein subcellular localization showed that MsrA protein was most likely located in the cytoplasm. Homology analysis showed that MsrA of V. alginolyticus had high homology with other Vibrio species, and the highest homology with V. alginolyticus. In the prediction of functional domains, MsrA had the function of methionine sulfoxide reduction. In secondary structure prediction, MsrA contained random coils at a proportion of 46.70%, which was the highest. The similarity between the tertiary structure model of MsrA and template Q87SW6. 1. A was 89. 15%. PTM analysis showed that MsrA protein had many PTM modification sites such as phosphorylation and glycosylation sites. [Conclusions] This study provides some reference value for further study on the role of MsrA in bacterial antioxidant stress. [ABSTRACT FROM AUTHOR]