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The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both Gram-positive and Gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan

机译：OmpA相关外膜蛋白和MotB之间的C端序列保守性表明，革兰氏阳性菌和革兰氏阴性菌都有共同的功能，可能是这些域与肽聚糖的相互作用

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status: published

机译：状态：已发布

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作者
De Mot René; Vanderleyden Jozef;
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年度 1994
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正文语种 en
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1. Peptidoglycan-associated outer membrane protein Mep45 of rumen anaerobe Selenomonas ruminantium forms a non-specific diffusion pore via its C-terminal transmembrane domain [J] . Kojima Seiji, Hayashi Kanako, Tochigi Saeko, Bioscience, Biotechnology, and Biochemistry . 2016,第10期

机译：爪子蛋白相关的外膜蛋白MEP45瘤胃anaerobe Selenomonas强者通过其C末端跨膜结构域形成非特异性扩散孔
2. Cadaverine Covalently Linked to Peptidoglycan Is Required for Interaction between the Peptidoglycan and the Periplasm-Exposed S-Layer-Homologous Domain of Major Outer Membrane Protein Mep45 in Selenomonas ruminantium [J] . Seiji Kojima, Kyong-Cheol Ko, Yumiko Takatsuka, Journal of bacteriology . 2010,第22期

机译：肽聚糖与主要外膜蛋白Mep45的硒外露瘤菌中周质暴露的S层同源域之间的相互作用需要与肽聚糖共价连接的尸胺。
3. The peptidoglycan-binding (PGB) domain of the Escherichia coli pal protein can also function as the PGB domain in E. coli flagellar motor protein MotB. [J] . Hizukuri Y, Morton JF, Yakushi T The Journal of Biochemistry . 2009,第2期

机译：大肠杆菌pal蛋白的肽聚糖结合（PGB）结构域还可以用作大肠杆菌鞭毛运动蛋白MotB中的PGB结构域。
4. Cadaverine Covalently Linked to Peptidoglycan Is Required for Interaction between the Peptidoglycan and the Periplasm-Exposed S-Layer-Homologous Domain of Major Outer Membrane Protein Mep45 in Selenomonas ruminantium [O] . Seiji Kojima, Kyong-Cheol Ko, Yumiko Takatsuka, 2010

机译：肽聚糖与主要外膜蛋白Mep45的Sermoomonas ruminantium的质膜暴露的S层-同源域之间的相互作用需要与肽聚糖共价连接的尸胺。
5. A family of Gram-negative bacterial outer membrane factors that function in the export of proteins, carbohydrates, drugs and heavy metals from Gram-negative bacteria [O] . Ian T Paulsen, Jay H Park, Peter S Choi, 2006

机译：一系列革兰氏阴性细菌外膜因子，可在革兰氏阴性细菌出口蛋白质，碳水化合物，药物和重金属的出口中的作用

The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both Gram-positive and Gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan

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