• DRAMP ID

    • DRAMP00234
    • Peptide Name

    • Trifolitoxin (TFX; Bacteriocin)
    • Source

    • Rhizobium leguminosarum bv. Trifolii T24 (Gram-negative bacteria)
    • Family

    • Not found
    • Gene

    • tfxA
    • Sequence

    • DIGGSRQGCVA
    • Sequence Length

    • 11
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial
    • Target Organism

    • No MICs found in DRAMP database
    • 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

    • Not found
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP00234 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP00234.
    • Formula

    • C41H71N15O16S
    • Absent Amino Acids

    • EFHKLMNPTWY
    • Common Amino Acids

    • G
    • Mass

    • 1062.17
    • PI

    • 5.83
    • Basic Residues

    • 1
    • Acidic Residues

    • 1
    • Hydrophobic Residues

    • 3
    • Net Charge

    • 0
    • Boman Index

    • -17.71
    • Hydrophobicity

    • -0.046
    • Aliphatic Index

    • 70.91
    • Half Life

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

    • 0
    • Absorbance 280nm

    • 0
    • Polar Residues

    • 5

DRAMP00234

    • Function

    • Antibiotic whose production provides the bacteria a mechanism of host root nodule competitiveness with other invading inefficient strains.
    • PTM

    • Synthesized ribosomally as a prepeptide that is post-translationally modified to the active peptide. TfxB, TfxD and TfxF are all required for this processing.The chromophore is probably a six-membered ring derived from the cyclization of Gln-38.
    • Maturation of thiazole and oxazole containing antibiotics involves the enzymic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline rings are dehydrogenated to form thiazole or oxazole rings.

    • Biophysicochemical properties

    • pH dependence (Sensitive to extremes of pH); Temperature dependence (Thermostable).
  • ·Literature 1
    • Title

    • DNA sequence and mutational analysis of genes involved in the production and resistance of the antibiotic peptide trifolitoxin.
    • Reference

    • J Bacteriol. 1993 Jun;175(12):3693-3702.
    • Author

    • Breil BT, Ludden PW, Triplett EW.