• DRAMP ID

    • DRAMP00183
    • Peptide Name

    • Thuricin-17 (Thurincin H; Bacteriocin)
    • Source

    • Bacillus thuringiensis (strain SF361/NEB17) (Gram-positive bacteria)
    • Family

    • Belongs to the class IId bacteriocin
    • Gene

    • tucA1
    • Sequence

    • DWTCWSCLVCAACSVELLNLVTAATGASTAS
    • Sequence Length

    • 31
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+
    • Target Organism

      • Gram-positive bacteria: Bacillus subtilis ATCC 6633 (++), Bacillus subtilis ATCC 6537 (+), Bacillus subtilis CU1065 5(WT) (+++), Bacillus subtilis LRB90 (+), Bacillus subtilis LRB91 (+), Bacillus cereus F4552 (+++++), Bacillus cereus F4810 (+++++), Bacillus cereus Northview P2E018 (+++++), Geobacillus stearothermophilus ATCC 12980 (+++++), Bacillus thuringiensis EG10368 (+++++), Bacillus megaterium LRB89 (+++++), Listeria mo nocytogenes F2 586 1053 (++++), Listeria monocytogenes 2289 (++++), Listeria innocua ATCC 2283 (+++++), Listeria ivanovii ATCC 19119 (+++++), Micrococcus luteus (+), Staphylococcus aureus ATCC 9144 (+), Staphylococcus aureus ATCC 8095 (+), Carnobacterium piscicola CU216 (+++++) [NOTE: + (weakly activity) to +++++ (highest activity)]
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Not found
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Alpha helix (2 helices; 18 residues)
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP00183 helical wheel diagram
    • PDB ID

    • 2LBZ resolved by NMR.
  • 2LBZ-> 
    • Predicted Structure

    • Formula

    • C134H212N34O45S4
    • Absent Amino Acids

    • FHIKMPQRY
    • Common Amino Acids

    • A
    • Mass

    • 3147.6
    • PI

    • 3.67
    • Basic Residues

    • 0
    • Acidic Residues

    • 2
    • Hydrophobic Residues

    • 15
    • Net Charge

    • -2
    • Boman Index

    • 7.33
    • Hydrophobicity

    • 0.965
    • Aliphatic Index

    • 97.74
    • Half Life

      • Mammalian:1.1 hour
      • Yeast:3 min
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 11250
    • Absorbance 280nm

    • 375
    • Polar Residues

    • 14

DRAMP00183

DRAMP00183 chydropathy plot
    • Function

    • The bacteriocin thurincin H, which is produced by Bacillus thuringiensis SF361, exhibits strong activity against a spectrum of Bacillus and Listeria spp. , including the human pathogen Listeria monocytogenes. The application of this bacteriocin to leaves (spray) or roots (drench) directly stimulates the growth of both a C(3) dicot (soybean) and a C(4) monocot (corn). This growth stimulation is similar in nature to that previously seen when plants are treated with Nod factors. Strain NEB17 contains three copies of the gene for thuricin 17 that code for identical amino acid sequences. These two lines of evidence suggest that the dual functions of these proteins may have constrained their evolution. This is the first report of direct plant growth enhancement by a bacteriocin.
  • ·Literature 1
    • Title

    • The Belongs to the class IId bacteriocin thuricin-17 increases plant growth.
    • Reference

    • Planta. 2009 Mar;229(4):747-755.
    • Author

    • Lee KD, Gray EJ, Mabood F, Jung WJ, Charles T, Clark SR, Ly A, Souleimanov A, Zhou X, Smith DL.
  • ·Literature 2
    • Title

    • A novel bacteriocin, thuricin 17, produced by plant growth promoting rhizobacteria strain Bacillus thuringiensis NEB17: isolation and classification.
    • Reference

    • J Appl Microbiol. 2006 Mar;100(3):545-554.
    • Author

    • Gray EJ, Lee KD, Souleimanov AM, Di Falco MR, Zhou X, Ly A, Charles TC, Driscoll BT, Smith DL.
  • ·Literature 3
    • Title

    • Biosynthesis and transcriptional analysis of thurincin H, a tandem repeated bacteriocin genetic locus, produced by Bacillus thuringiensis SF361.
    • Reference

    • FEMS Microbiol Lett. 2009 Oct;299(2):205-213.
    • Author

    • Lee H, Churey JJ, Worobo RW.
  • ·Literature 4
    • Title

    • The 3D solution structure of thurincin H, a bacteriocin with four sulfur to alpha-carbon crosslinks.
    • Reference

    • Angew Chem Int Ed Engl. 2011 Sep 5;50(37):8718-8721.
    • Author

    • Sit CS, van Belkum MJ, McKay RT, Worobo RW, Vederas JC.