大额牛瘤胃细菌CMC-1蛋白结构和功能的生物信息学分析  

Bioinformatics analysis of protein structure and function of CMC-1 from rumen bacteria of Gayal (Bos frontalis)

作　　者：张光荣 袁再美 孙丽媛 邓茗月 王荣蛟 和世春[1,2] 王寒雪 毛华明 杨舒黎[1,2] ZHANG Guangrong;YUAN Zaimei;SUN Liyuan;DENG Mingyue;WANG Rongjiao;HE Shichun;WANG Hanxue;MAO Huaming;YANG Shuli(Faculty of Animal Science and Technology,Yunnan Agricultural Iniversity,Kunming 650201,China;Yunnan Provincial Key Laboratory of Animal Nutrition and Feed Science,Kunming 650201,China;Kunming Center for Disease Control and Prevention,Kunming 650223,China)

机构地区：[1]云南农业大学动物科学技术学院,昆明650201 [2]云南省动物营养与饲料科学重点实验室,昆明650201 [3]昆明市动物疫病预防控制中心,昆明650223

出　　处：《黑龙江畜牧兽医》2021年第3期16-21,157,共7页Heilongjiang Animal Science And veterinary Medicine

基　　金：云南省重点研发计划项目(2018BB001);云南省农业基础联合专项(2017FG001[-061])。

摘　　要：为了深入了解大额牛瘤胃细菌CMC-1蛋白的结构和功能,试验利用ProtParam、TMHMM Server 2.0、ProtScale、NCBI Conserved Domains、SignalP 5.0、TargetP、PSORTⅡserver、SOPMA、SWISS-MODEL、NCBI protein BLASTp和MEGA 7.0等在线工具和软件,对CMC-1蛋白的理化性质、跨膜区、亲水性/疏水性、结构域、信号肽及亚细胞定位、二级结构、三级结构、系统进化等内容进行分析。结果表明:CMC-1蛋白的相对分子质量为47 026.01,理论等电点为5.68,带负电荷的残基总数为49个,带正电荷的残基总数为41个,估计半衰期为100 h,属于亲水型稳定的跨膜脂蛋白,定位于线粒体中,含有一个主要由α-螺旋、无规则卷曲、扩展链、β-转角组成的保守结构域,三级结构同源建模有较高的置信度;CMC-1蛋白在进化树中独立成支,与普雷沃氏菌科细菌HUN156糖苷水解酶家族5中的纤维素酶蛋白同源性较高。说明CMC-1蛋白是与普雷沃氏菌科细菌HUN156纤维素酶蛋白有较高亲缘关系的亲水型跨膜脂蛋白,可能来源于一个新的微生物种或一个新的纤维素酶基因。In order to further understand the structure and function of CMC-1 protein in rumen bacteria of Gayal(Bos frontalis), online tools and software such as ProtParam, TMHMM Server 2.0, ProtScale, NCBI Conserved Domains, SignalP 5.0, TargetP, PSORTⅡ server, SOPMA, SWISS-MODEL, NCBI protein BLASTp and MEGA 7.0 were used to analyzed the physical and chemical properties, transmembrane region, hydrophilicity/hydrophobicity, domain, signal peptide and subcellular localization, secondary structure, tertiary structure and system evolution of CMC-1 protein. The results showed that the relative molecular weight of CMC-1 protein was 47 026.01, the theoretical isoelectric point was 5.68, the total number of residues with negative charge was 49, the total number of residues with positive charge was 41, and the estimated half-life was 100 h, which belonged to hydrophilic stability. The identified transmembrane lipoproteins, located in mitochondria, contained a conserved domain mainly composed of α helix, irregular curl, a small amount of extended strand and β turning angle. The three-dimensional structure homology modeling had a high degree of confidence. The CMC-1 protein was independently branched in the phylogenetic tree, and had high homology with cellulose which belonged to the glycoside hydromassage family 5 protein of Prevotellaceae bacteria HUN156. It indicated that CMC-1 protein was a hydrophilic transmembrane lipoprotein with a high relationship with the cellulose of Preunellaceae bacteria HUN156, which might be derived from a new species of microorganism or a new cellulase gene.

关 键 词：大额牛 瘤胃细菌 CMC-1蛋白 蛋白质结构 蛋白质功能 生物信息学分析 

分 类 号：S823[农业科学—畜牧学] S852.6[农业科学—畜牧兽医]