| 引用本文: | 王文靖,孙妍,王心倩,余晓丽.鸟胞内分枝杆菌mmpL11同源基因序列分析及功能预测[J].生物信息学,2016,14(1):7-12. |
| WANG Wenjing,SUN Yan,WANG Xinqian,YU Xiaoli.Sequence analysis and function prediction of Mycobacterium aviumintracellulare mmpL11gene[J].Chinese Journal of Bioinformatics,2016,14(1):7-12. |
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| 摘要: |
| 以非结核分枝杆菌中的胞分枝杆菌、鸟分枝杆菌两个标准株为研究对象,以耻垢分枝杆菌mc2 155和结核分枝杆菌H37Rv为对照,对其mmpL11同源基因进行序列分析,并对其蛋白质进行结构及功能预测,为后期的抗酸染色阳性菌诊断,药物靶标的筛选提供理论基础。根据同源比对找到两个标准株的mmpL11同源基因；应用expasy工具预测MmpL11同源蛋白理化性质；蛋白质信号肽预测采用SignalP在线软件进行预测；使用TMHMM在线工具进行拓扑结构预测；利用Interproscan工具对蛋白保守序列和功能进行预测；使用SSpro对蛋白二级结构进行预测。OCU48920蛋白的理化性质分析显示:其氨基酸个数为1 018,分子量为108.4 kD,理论等电点为7.61,疏水指数为0.227；MAP3637c蛋白的理化性质分析显示:其氨基酸个数为1 007,分子量为107.2 kD,理论等电点为8.59,疏水指数为0.231。信号肽预测发现两个标准株的MmpL11均不存在信号肽切割位点,未发现信号肽存在。跨膜预测发现其跨膜次数分别为12和12肽链,N端均在膜内,二级结构以α-螺旋和β-片层为主。保守序列预测发现两个标准株的MmpL11蛋白均有两个MMPL跨膜结构域,一个固醇敏感多肽区。OCU48920、 MAP3637c为H37Rv的MmpL11同源蛋白,推测其功能同MmpL11相似,是分枝菌酸的转运蛋白,参与胞内小分子的运输和信号转导。 |
| 关键词: 非结核分枝杆菌 MmpL11 序列分析 功能预测 |
| DOI：10.3969/j.issn.1672-5565.2016.01.02 |
| 分类号:Q 93 |
| 文献标识码:A |
| 基金项目:武汉轻工大学研究生创新基金项目(2014cx019)。 |
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| Sequence analysis and function prediction of Mycobacterium aviumintracellulare mmpL11gene |
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WANG Wenjing1 , SUN Yan2, WANG Xinqian2, YU Xiaoli2
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(1.The Second Middle School Nanyang, Nanyang 473000, China; 2.School of Biology and Pharmaceutical Engineering, Wuhan Polytechnic University, Wuhan 430023, China)
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| Abstract: |
| To provide evidence for future research on the structures and function of mmpL11(Rv0202c) in Mycobacterium, we analyzed homologous sequences, predicted topological structures and conservative domain structures of two Nontuberculous Mycobacterionsnamed M. Intracellulareand M.avium, both of which were compared with M.SmegmatisstrMC2155 and H37Rv. According to the homologous comparison,we found two standard strains of mmpL11homologous genes. The physicochemical properties and con-served domain of MmpL11 in M. tuberculosiswere predicted by ExPASy online tools. Online tool TMHMM Server 2.0 was used to predicted the topological structure.Interproscan was used to predict conservative domain structure. SSpro was used to predict the secondary structure． According to the physical and chemical properties of protein, the amino acid number of OCU48920 was 1 018, molecular weight was 108.4 kD, theoretical isoelectric point was 7.61,hydrophobic index was 0.227, the amino acid number of MAP3637c was 1 007, the molecular weight was 107.2 kD, theoretical isoelectric point was 8.59, hydrophobic index was 0.231,the amino acid number of MSMEG0241 was 954, the molecular weight was 102.6 kD, theoretical isoelectric point was 5.98 and hydrophobic index was 0.305.By SignalP’spredicting,we found MmpL11 didnt have signal peptide cutting locus in its three standard strains and signal peptide.The forecast of transmembrane showed that it crossed membrane 12 times and 12 peptides.N-terminal was within the membrane.Secondary structure was given priority to with alpha helix and beta patches.The prediction of conservative sequence and MmpL11 protein’s function showed two MMPL transmembrane domain (MMPL domain) structure, a sterol sensitive polypeptide area (SSD domain). OCU48920, MAP3637c were homologous proteins of H37Rv MmpL11.We speculate that their functions were similar with MmpL11, and they were transcators of mycolic-acid.These two proteins participated in transporting intracellular small molecules and signal transduction. |
| Key words: Nontuberculous Mycobacterion MmpL11 Sequential analysis Function prediction |
