Bioinformatics Analysis of OmpA/MotB Protein Encoded by OmpA/MotB Gene(ORF 648bp) of Riemerella anatipestifer

Abstract:

The OmpA/MotB gene from RA by our lab was sequenced. And the molecular characteristic of this gene was analyzed with bioinformatics software. The results indicated that this gene encodes an estimated 215 protein, contains the conserved domain of the OmpA-like protein. The relative molecular weight of the protein was 23.34525kDa, and there is no signal peptide and transmembrane region of the protein. One cAMP-and cGMP-dependent protein kinase phosphorylation site, six Protein kinase C phosphorylation sites, five Casein kinase II phosphorylation sites, five N-myristoylation sites and antigenic determinants were searched in the protein. Most of the total proteins were located in the Outer membrane and cytoplasmic. Phylogenetic tree of the amino acids sequences showed this gene has a close evolutionary relationship with Elizabethkingia anopheles Ag1 and Weeksella virosa DSM16922, indicating that the RA OmpA/MotB protein may have some similar functions with them. These results provided rational data to elucidate biological function and physiological features of the protein.

• Periodical: Advanced Materials Research (Volume 647)
• Pages: 304-309
• DOI: https://doi.org/10.4028/www.scientific.net/AMR.647.304
• Online since: January 2013
• Authors: Xu Pan, An Chun Cheng, Ming Shu Wang, De Kang Zhu, Xiao Jia Wang
• Keywords: Bioinformatics, OmpA/MotB Protein, RA, Sequence Analysis

References

[1] P. Segers, W. Mannheim, M. Vancanneyt, K. De. Brandt, K.H. Hinz, K. Kersters and P. Vandamme: Syst. Bacterio Vol. 1 (1993), pp.768-776.

[2] C.F. Chang: Vet Med Anim Hus Vol. 43 (1984), pp.40-46.

[3] T.S. Sandhu: Diseases of Poultry Vol. 12 (2008), pp.758-764.

[4] M. Bisgaard: Avian Pathol Vol. 11 (1982), pp.341-350.

[5] H. Loh, T.P. Teo and H.C. Tan: Avian Pathol Vol. 21 (1992), pp.453-459.

[6] T.S. Sandhu and M.L. Lesiter: Avian Pathol Vol. 20 (1991), pp.233-239.

[7] P. Pathanasophon, P. Phuektes, T. Tanticharoenyos, W. Narongsak and T. Sawada: Avian Pathol Vol. 31(2002), pp.267-270.

DOI: 10.1080/03079450220136576

[8] Y.P. Chen, S.H. Lee, C.H. Chou and H.J. Tsai: Vet. Microbiol Vol. 154 (2012), pp.325-331.

[9] C.Y. Zhong, A.C. Cheng, M. S, Wang, D.K. Zhu, Q.H. Luo, C.D. Zhong, L. Li and Z. Duan,: Avian Dis Vol. 53 (2009), pp.601-607.

[10] S. Subramaniam, B. Huang, H. Loh, J. Kwang, H.M. Tan, K.L. Chua and J. Frey: Immunol Vol. 7 (2000), pp.168-174.

[11] K.C. Crasta, K.L. Chua, S. Subramaniam, J. Frey, H. Loh and H.M. Tan: Bacteriol Vol. 184 (2002), p.1832-(1939).

[12] Q. Hu, X. Han, C. Ding, Y. Zhu, S. Yu: Vet. Microbiol Vol. 150 (2011), pp.278-283.

[13] A. C. cheng, M. S. wang, X. Y. chen, D. K. zhu, C. huang, F. liu, Y. zhou, Y. F. guo, Z. Y. liu, and P. F. fang: Chinese Journal of Veterinary Science Vol. 23 (2003), pp.320-232.

[14] X. J. Wang, D. K. Zhu, M.S. Wang, A.C. Cheng, R.Y. Jia, Y. Zhou, Z.L. Chen, Q.H. Luo, F. Liu, Y. Wang and X.Y. Chen: Bacteriology Vol. 194 (2012), pp.3270-3271.

DOI: 10.1128/jb.00366-12

[15] S.F. Altschul, T.L. Madden, A.A. Schaffer, J. Zhang, Z. Zhang, W. Miller and D.J. Lipman: Nucleic Acids Res Vol. 25 (1997), pp.3389-3402.

[16] E.L. Sonnhammer von, G. Heijne and A. Krogh: Proc Int Conf Intell Syst Mol Biol Vol. 6 (1998), pp.175-182.

[17] A.S. Kolaskar and P.C. Tongaonkar: FEBS Lett Vol. 276 (1990), pp.172-174.

[18] J. Kyte and R.F. Doolittle: Mol Biol Vol. 157 (1982), pp.105-132.

[19] A. Kishimoto, K. Nishiyama, H. Nakanishi, Y. Uratsuji, H. Nomura, Y. Takeyama and Y. Nishizuka: Biol Chem Vol. 260 (1985), pp.12493-12499.

DOI: 10.1016/s0021-9258(17)38898-1