PMID:7592387
| Citation |
Begg, KJ, Dewar, SJ and Donachie, WD (1995) A new Escherichia coli cell division gene, ftsK. J. Bacteriol. 177:6211-22 |
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| Abstract |
A mutation in a newly discovered Escherichia coli cell division gene, ftsK, causes a temperature-sensitive late-stage block in division but does not affect chromosome replication or segregation. This defect is specifically suppressed by deletion of dacA, coding for the peptidoglycan DD-carboxypeptidase, PBP 5. FtsK is a large polypeptide (147 kDa) consisting of an N-terminal domain with several predicted membrane-spanning regions, a proline-glutamine-rich domain, and a C-terminal domain with a nucleotide-binding consensus sequence. FtsK has extensive sequence identity with a family of proteins from a wide variety of prokaryotes and plasmids. The plasmid proteins are required for intercellular DNA transfer, and one of the bacterial proteins (the SpoIIIE protein of Bacillus subtilis) has also been implicated in intracellular chromosomal DNA transfer. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins; Base Sequence; Binding Sites; Carrier Proteins/genetics; Cell Division/genetics; Chromosome Mapping; Consensus Sequence; Escherichia coli/cytology; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins; Genes, Bacterial; Genetic Complementation Test; Hexosyltransferases; Membrane Proteins/genetics; Molecular Sequence Data; Muramoylpentapeptide Carboxypeptidase/genetics; Mutation; Penicillin-Binding Proteins; Peptidoglycan/biosynthesis; Peptidyl Transferases; Phenotype; Protein Structure, Secondary; Recombination, Genetic; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Suppression, Genetic |
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Significance
This is the original description of the ftsK mutant TOE44.
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