General Information

    • DRAMP ID

    • DRAMP18336

    • Peptide Name

    • Thermophilin 1277 (Bacteriocin)

    • Source

    • Streptococcus thermophilus SBT1277

    • Family

    • Belongs to the lantibiotics family (Class I bacteriocin)

    • Gene

    • tepA

    • Sequence

    • ADRGWIKTLTKDCPNVISSICAGTIITACKNCA

    • Sequence Length

    • 33

    • Protein Existence

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial, Anti-Gram+

    • Target Organism

    • Gram-positive

    • 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

    • Rich

    • Structure Description

    • Peptide sequence analysis following chemical modification of thermophilin 1277 revealed that the Cys21 and Cys29 residues form a disulfide bridge and that Thr8 or Thr10 forms two 3-methyllanthionines with Cys13 or Cys32 via thioether bridges. Antimicrobial activity was disrupted by ethanethiol or reductive agent treatments, indicating that the internal amino acid modifications are crucial for the activity.

    • Helical Wheel Diagram

    • DRAMP18336 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP18336.

Physicochemical Information

    • Formula

    • C147H248N42O46S4

    • Absent Amino Acids

    • EFHMQY

    • Common Amino Acids

    • I

    • Mass

    • 3468.08

    • PI

    • 8.53

    • Basic Residues

    • 4

    • Acidic Residues

    • 2

    • Hydrophobic Residues

    • 12

    • Net Charge

    • +2

    • Boman Index

    • -2924

    • Hydrophobicity

    • 0.297

    • Aliphatic Index

    • 91.82

    • Half Life

      • Mammalian:4.4 hour
      • Yeast:>20 hour
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 5750

    • Absorbance 280nm

    • 179.69

    • Polar Residues

    • 14

DRAMP18336

DRAMP18336 chydropathy plot

Comments Information

    • It shares the same sequence with bovicin HJ50 prior to post-translational modifications. A followup study concluded at two rings and one disulfide bond .

Literature Information

  • ·Literature 1

    • Title

    • Characterization of a bacteriocin, Thermophilin 1277, produced by Streptococcus thermophilus SBT1277.

    • Reference

    • J Appl Microbiol. 2007 Apr;102(4):971-80.

    • Author

    • Kabuki T, Uenishi H, Watanabe M, Seto Y, Nakajima H.