General Information

    • DRAMP ID

    • DRAMP00162

    • Peptide Name

    • Thuricin CDalpha (Trn-alpha; one peptide of Thuricin CD; Bacteriocin)

    • Source

    • Bacillus thuringiensis DPC 6431 (Gram-positive bacteria)

    • Family

    • Belongs to the class IIb bacteriocin

    • Gene

    • Not found

    • Sequence

    • GNAACVIGCIGSCVISEGIGSLVGTAFTLG

    • Sequence Length

    • 30

    • Protein Existence

    • Predicted

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+

    • Target Organism

      • Gram-positive bacteria: Clinical Clostridium difficile isolates (MIC in the range of nM) and Listeria monocytogenes, Lactobacillus fermentum.

    • Hemolytic Activity

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

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Not found

Structure Information

    • 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 (3 helices; 16 residues)

    • Structure Description

    • Trn-α has L-stereochemistry at Ser21 (alpha-R), L-stereochemistry at Thr25 (alpha-R), and D-stereochemistry at Thr28 (alpha-S) (an LLD isomer).

    • Helical Wheel Diagram

    • DRAMP00162 helical wheel diagram

    • PDB ID

    • 2L9X resolved by NMR.
  • 2L9X-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP00162.

Physicochemical Information

    • Formula

    • C118H197N31O39S3

    • Absent Amino Acids

    • DHKMPQRWY

    • Common Amino Acids

    • G

    • Mass

    • 2770.23

    • PI

    • 4

    • Basic Residues

    • 0

    • Acidic Residues

    • 1

    • Hydrophobic Residues

    • 13

    • Net Charge

    • -1

    • Boman Index

    • 31.68

    • Hydrophobicity

    • 1.343

    • Aliphatic Index

    • 117

    • Half Life

      • Mammalian:30 hour
      • Yeast:>20 hour
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 125

    • Absorbance 280nm

    • 4.31

    • Polar Residues

    • 16

DRAMP00162

DRAMP00162 chydropathy plot

Comments Information

    • Function

    • Thuricin CD is produced by Bacillus thuringiensis DPC 6431, a bacterial strain isolated from a human fecal sample, and it consists of two distinct peptides, Trn-alpha and Trn-beta, that act synergistically to kill a wide range of clinical C. difficile isolates. Thuricin CD showes no activity against any Gram-negative organisms tested, including Escherichia coli, Pseudomonas sp., Salmonella sp., and Bacteroides fragilis.

    • Biophysicochemical properties

    • Cell-free supernatants of thuricin were active throughout the pH range of 2-9 and heat stable up to 85 °C. There was, however, a reduction in activity at 90 °C and a complete loss of activity at 100 °C after 15 min.

Literature Information

  • ·Literature 1

    • Title

    • Thuricin CD, a posttranslationally modified bacteriocin with a narrow spectrum of activity against Clostridium difficile.

    • Reference

    • Proc Natl Acad Sci U S A. 2010 May 18;107(20):9352-9357.

    • Author

    • Rea MC, Sit CS, Clayton E, O'Connor PM, Whittal RM, Zheng J, Vederas JC, Ross RP, Hill C.
  • ·Literature 2

    • Title

    • The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to alpha-carbon cross-links.

    • Reference

    • J Am Chem Soc. 2011 May 25;133(20):7680-7683.

    • Author

    • Sit CS, McKay RT, Hill C, Ross RP, Vederas JC.