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PMID:10922461
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| Citation |
Dorazi, R and Dewar, SJ (2000) Membrane topology of the N-terminus of the Escherichia coli FtsK division protein. FEBS Lett. 478:13-8 |
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| Abstract |
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. |
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| Keywords |
Alkaline Phosphatase/genetics; Alkaline Phosphatase/metabolism; Amino Acid Motifs; Amino Acid Substitution; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Biological Transport; Cell Division; Cell Membrane/chemistry; Cell Membrane/metabolism; Computer Simulation; Conserved Sequence/genetics; Escherichia coli/chemistry; Escherichia coli/cytology; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Mutation; Protein Structure, Tertiary; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Temperature; beta-Galactosidase/genetics; beta-Galactosidase/metabolism |
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