J 1999

Characterization of colicin S4 and its receptor, OmpW, a minor protein of

PILSL, H., David ŠMAJS and V. BRAUN

Basic information

Original name

Characterization of colicin S4 and its receptor, OmpW, a minor protein of

Authors

PILSL, H., David ŠMAJS and V. BRAUN

Edition

J. Bacteriol. 1999

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Germany

Confidentiality degree

není předmětem státního či obchodního tajemství

Organization unit

Faculty of Medicine
Změněno: 24/1/2003 12:28, prof. MUDr. David Šmajs, Ph.D.

Abstract

V originále

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 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.