General Information

    • DRAMP ID

    • DRAMP00133

    • Peptide Name

    • Lactococcin G subunit beta (Gbeta ; Bacteriocin)

    • Source

    • Lactococcus lactis subsp. lactis (Streptococcus lactis) (Gram-positive bacteria)

    • Family

    • Belongs to the class IIb bacteriocin

    • Gene

    • Not found

    • Sequence

    • KKWGWLAWVDPAYEFIKGFGKGAIKEGNKDKWKNI

    • Sequence Length

    • 35

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial

    • Target Organism

    • Lactococcus.

    • 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

    • Structure Description

    • In DPC, LcnG-beta has an N-terminal alpha-helix (residues 6-19). The region from residues 20 to 35, which also contains a flexible GxxxG-motif (residues 18-22), appeared to be fairly unstructured in DPC.

    • Helical Wheel Diagram

    • DRAMP00133 helical wheel diagram
  • 2JPK-> 

    • Predicted Structure

    • There is no predicted structure for DRAMP00133.

Physicochemical Information

    • Formula

    • C198H291N49O47

    • Absent Amino Acids

    • CHMQRST

    • Common Amino Acids

    • K

    • Mass

    • 4109.79

    • PI

    • 9.7

    • Basic Residues

    • 8

    • Acidic Residues

    • 4

    • Hydrophobic Residues

    • 14

    • Net Charge

    • +4

    • Boman Index

    • -39.75

    • Hydrophobicity

    • -0.806

    • Aliphatic Index

    • 61.43

    • Half Life

      • Mammalian:1.3 hour
      • Yeast:3 min
      • E.coli:2 min

    • Extinction Coefficient Cystines

    • 23490

    • Absorbance 280nm

    • 690.88

    • Polar Residues

    • 8

DRAMP00133

DRAMP00133 chydropathy plot

Comments Information

    • MOA

    • The N-terminal halves of both the alpha and beta peptides may form amphiphilic alpha-helices, suggesting that the peptides are pore-forming toxins that create cell membrane channels through a "barrel-stave" mechanism. Bacteriocin activity requires interaction of alpha and beta peptides in a molar ratio of 7

Literature Information

  • ·Literature 1

    • Title

    • A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides.

    • Reference

    • J Bacteriol. 1992 Sep;174(17):5686-5692.

    • Author

    • Nissen-Meyer J, Holo H, H¥varstein LS, Sletten K, Nes IF.
  • ·Literature 2

    • Title

    • Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin lactococcin G.

    • Reference

    • Biochim Biophys Acta. 2008 Mar;1784(3):543-554.

    • Author

    • Rogne P, Fimland G, Nissen-Meyer J, Kristiansen PE.