Characterization of colicin S4 and its receptor, OmpW, a minor protein of the Escherichia coli outer membrane

被引：88

作者：

Pilsl, H ^{[1
]}

Smajs, D ^{[1
]}

Braun, V ^{[1
]}

机构：

[1] Univ Tubingen, Tubingen, Germany

来源：

JOURNAL OF BACTERIOLOGY | 1999年 / 181卷 / 11期

关键词：

D O I：

10.1128/JB.181.11.3578-3581.1999

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Analysis of the nucleotide sequence of an Escherichia coli colicin S4 determinant revealed 76% identity to the pore-forming domain of the colicin A protein, 77% identity to the colicin A immunity protein, and 82% identity to the colicin A lysis protein. The N-terminal region, which is responsible for the Tol-dependent uptake of colicin S4, has 93% identity to the N-terminal region of colicin K. By contrast, the predicted receptor binding domain shows no sequence similarities to other colicins. Mutants that lacked the OmpW protein were resistant to colicin S4.

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页码：3578 / 3581

页数：4

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