Objective To investigate the physicochemical properties and functional prediction of S.pneumoniae spr1759 protein in purulent meningitis.Methods The relevant sequence information of spr1759 protein was obtained from NCBI database.The physical and chemical characteristics and hydrophobicity of spr1759 protein were analyzed by ProtParam and ProtScale.The phosphorylation site and transmembrane region structure of spr1759 were analyzed by NetPhos and TMHMM.The secondary structure and tertiary structure of spr1759 protein were predicted by SOPMA,SWISS-MODEL,and ABCpred,respectively.The epitope prediction analysis was performed using SYFPEITHI software.The interacting protein of spr1759 was predicted using STRING,and its biological process was functionally enriched and analyzed.Results spr1759 protein was a hydrophilic protein with an isoelectric point of 5.11 and a transmembrane region,all of which contained a transmembrane structure.S.pneumoniae spr1759 protein belonged to the LytRcpsApsr superfamily and may be an enzyme involved in anionic cell wall polymer synthesis.The amino acid sequence of S.pneumoniae spr1759 protein was highly homologous to B.anthracis BAS5115 protein and B.subtilis DJ971211 protein,with 35.7％and 32.5％full-length sequence similarity.Conclusion Streptococcus pneumoniae spr1759 protein is a hydrophilic protein with transmembrane structure and may have enzymatic functions related to anionic cell wall polymer synthesis.
关键词
脑膜炎/肺炎链球菌/spr1759蛋白/理化性质/蛋白功能预测
Key words
Meningitis/Streptococcus pneumoniae/spr1759 protein/Physicochemical properties/Protein function prediction
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