The bioinformatics analysis of the EF-TuMp

Mycoplasma pneumoniae has very limited metabolic and biosynthetic activities for proteins, carbohydrates, and lipids in comparison to common bacteria and causes clinical manifestations and has different tissue predilections. The surface-localized M. pneumoniae elongation factor Tu (EF-TuMp) mediates binding to the extracellular matrix component fibronectin via the carboxyl region of EF-Tu. M. pneumoniae surface-associated elongation factor Tu and the pyruvate dehydrogenase E1 beta subunit interact with fibronectin. In relation to get Elongation factor Tu protein sequence, uniprot database was used and its protein properties such as amino acid composition, theoretical PI, transmembrane domains, signal peptide and other properties were analyzed by online bioinformatics tools. The results revealed that this protein is classified as a stable protein with 29.05 index and is a cytosolic protein. Regarding to the second structure it possesses 19 beta sheets and 7 alpha-helixes. Since EF-Tu is one of the prokaryotic elongation factors, which are part of the mechanism that synthesizes new proteins by translation at the ribosome, so its protein bioinformatics analysis can be useful. Based on the analysis this protein has not any signal peptide in its N-termina

Keywords:

Bionformatic analysis , EF-TU , M. pneumonia