title: The life-cycle proteins RodA of Escherichia coli and SpoVE of Bacillus subtilis have very similar primary structures.
abstract: Comparison of the predicted amino acid sequence of the cell-cycle RodA protein with the National Research Foundation protein sequence database shows that the 370-amino-acid RodA, a protein that is essential for wall elongation in Escherichia coli and maintenance of the rod shape of the cell, is highly analogous, in terms of primary structure, with the Bacillus subtilis SpoVE protein involved in stage V of sporulation.
authors.affiliation: Service de Microbiologie, Université de Liège, Sart Tilman, Belgium.
authors.forename: B
authors.initials: B
authors.lastname: Joris
authors.forename: G
authors.initials: G
authors.lastname: Dive
authors.forename: A
authors.initials: A
authors.lastname: Henriques
authors.forename: P J
authors.initials: PJ
authors.lastname: Piggot
authors.forename: J M
authors.initials: JM
authors.lastname: Ghuysen
mesh_terms: D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000235:genetics*; D001426:Bacterial Proteins / Q000235:genetics*; D002473:Cell Wall / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D007256:Information Systems; D008565:Membrane Proteins / Q000235:genetics*; D008969:Molecular Sequence Data; D005810:Multigene Family
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; C064532:SpoVE protein, Bacillus subtilis; C061683:mrdB protein, E coli