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

ABSTRACT: 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 94% 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.

SUBMITTER: Pilsl H

PROVIDER: S-EPMC93827 | biostudies-literature | 1999 Jun

REPOSITORIES: biostudies-literature

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

Pilsl H H Smajs D D Braun V V

Journal of bacteriology 19990601 11

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 94% identity to the N-terminal region of colicin K. By contrast, the predicted receptor binding domain shows no sequence similarities to other colicins. M ...[more]

PMID: 10348872

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