title: Predictions of flexible C-terminal tethers of bacterial proteins with the FLEXTAIL bioinformatics pipeline.
abstract: Proteins use conserved binding motifs associated with relatively unconserved flexible amino acid sequences as mobile tethers for interacting molecules, as exemplified by C-terminal sequences of bacterial chemotaxis receptors. The FLEXTAIL bioinformatics pipeline predicts flexible tethers and their binding motifs based on the properties of flexibility and sequence conservation. In four groups of bacterial genomes, the algorithm identified > 100 putative binding domains, including verifying the known bacterial chemotaxis receptor-- NWETF binding motif. Some potential C-terminal flexible regions that have not previously been recognised to function as protein tethers were found and should be investigated further for binding targets and flexibility.
authors.affiliation: Computer Science Department, Prairie View A&M University, Prairie View, TX 77446, USA. yilu@pvamu.edu
authors.forename: Yi
authors.initials: Y
authors.lastname: Lu
authors.forename: Jeffrey L
authors.initials: JL
authors.lastname: Ram
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites / Q000235:genetics; D019295:Computational Biology; D003198:Computer Simulation; D017124:Conserved Sequence; D057225:Data Mining; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D054730:Protein Interaction Domains and Motifs / Q000235:genetics; D016415:Sequence Alignment / Q000706:statistics & numerical data; D017386:Sequence Homology, Amino Acid
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; C057635:Tsr protein, Bacteria