Membrane topology of the N-terminus of the Escherichia coli FtsK division protein

Robert Dorazi, Susan J. Dewar

    Research output: Contribution to journalArticlepeer-review

    28 Citations (Scopus)


    The Escherichia coli FtsK protein targets the septum, is essential for cell division and may play a role in DNA partitioning. Computer modelling suggests that the first 180 amino acids of the protein are embedded in the cytoplasmic membrane by up to six transmembrane domains. We demonstrate, using gene fusions, that the N-terminus contains four transmembrane helices that link two periplasmic domains. The first periplasmic domain contains an HEXXH amino acid sequence characteristic of zinc metalloproteases. We show by mutation analysis that the conserved glutamic acid of the HEXXH sequence is essential for FtsK function during septation. Copyright (C) 2000 Federation of European Biochemical Societies.

    Original languageEnglish
    Pages (from-to)13-18
    Number of pages6
    JournalFEBS Letters
    Issue number1-2
    Publication statusPublished - 28 Jul 2000


    • Cell division
    • FtsK
    • Metalloprotease
    • PhoA
    • Topology
    • Transmembrane


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