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.

引用

页码：3578 / 3581

页数：4

共 24 条

[1] The regulated outer membrane protein Omp21 from Comamonas acidovorans is identified as a member of a new family of eight-stranded β-sheet proteins by its sequence and properties [J].