• • DRAMP ID

  • DRAMP02473

• • Peptide Name

  • Cathelicidin-BF (Cathelicidin-related protein; Snakes, reptiles, animals)

• • Source

  • Bungarus fasciatus (Banded krait)

• • Family

  • Not found

• • Gene

  • Not found

• • Sequence

  • KFFRKLKKSVKKRAKEFFKKPRVIGVSIPF

• • Sequence Length

  • 30

• • UniProt Entry

  • B6D434

• • Protein Existence

  • Protein level

• • Biological Activity

  • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal

• • Target Organism

  • • [Ref.18795096]Gram-negative bacteria: Pseudomonas aeruginosa ATCC27853 (MIC=1.2 µg/ml), P. aeruginosa IS/DR (MIC=2.3 µg/ml), P. aeruginosa 08031205 IS/DR (MIC=9.4 µg/ml), P. aeruginosa 08031014 IS/DR (MIC=18.7 µg/ml), Escherichia coli ATCC25922 (MIC=2.3 µg/ml), E. coli 08A852 IS/DR (MIC=1.2 µg/ml), E. coli 08A866 IS/DR (MIC=0.6 µg/ml), E. coli 08031017 IS/DR (MIC=2.3 µg/ml), E. coli 08032813 IS/DR (MIC=2.3 µg/ml), E. coli 08040726 IS/DR (MIC=0.6 µg/ml), E. coli 08040722 IS/DR (MIC=0.6 µg/ml), Klebsiella pneumoniae IS/DR (MIC=4.7 µg/ml), K. pneumoniae 08031012 IS/DR (MIC=9.4 µg/ml), K. pneumoniae 08040202 IS/DR (MIC=0.6 µg/ml), K. pneumoniae 08040724 IS/DR (MIC=0.3 µg/ml), Pseudomonas luteola (MIC=1.2 µg/ml), Salmonella Typhi IS/DR (MIC=1.2 µg/ml), Acinetobacter calcoaceticus (MIC=2.3 µg/ml), Sphingobacterium siyangense (MIC=9.4 µg/ml), Saccharibacillus kuerlensis (MIC=4.7 µg/ml);
    • Gram-positive bacteria: Bacillus subtilis (MIC=9.4 µg/ml), B. pumilus (MIC=9.4 µg/ml), B. cereus (MIC=1.2 µg/ml), Staphylococcus aureus ATCC2592 (MIC=4.7 µg/ml), S. aureus 08A875 IS/DR (MIC=75 µg/ml), S. aureus 08031002 IS/DR (MIC>100 µg/ml), S. aureus 08031013 IS/DR (MIC>100 µg/ml), S. aureus 08032706 IS/DR (MIC>100 µg/ml), S. aureus 08032712 IS/DR (MIC>100 µg/ml), S. aureus 08032810 IS/DR (MIC>100 µg/ml), Enterococcus faecium IS/DR (MIC=150 µg/ml);
    • Fungi: Aspergillus terreus GIM3.34 (MIC=18.7 µg/ml), Aspergillus nidulans (MIC=18.7 µg/ml), Candida albicans ATCC2002 (MIC=4.7 µg/ml), Pichia pastoris (MIC=0.3 µg/ml).

• • Hemolytic Activity

  • • [Ref.18795096]Non-hemolytic activity at 400 µg/ml against human red blood cells

• • Cytotoxicity

  • • Not included yet

• • Binding Target

  • Cell membrane

• • 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

  • Not found

• • Helical Wheel Diagram

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP02473.

DRAMP02473

• • Function

  • Adopts an amphipathic alpha helical conformation, that may allow to partition into the target membrane. No hemolytic and cytotoxic activities have been observed on mammalian cells.

• • Tissue specificity

  • Expressed by the venom gland, stomach, trachea, skin, muscle, heart, kidney, lung, brain, intestine, spleen, liver, and ovary.

• • Miscellaneous

  • A predicted cleavage site is located at position Val-157-158-Lys, giving a peptide of 34 residues instead of the 30 residues found for the purified protein. The 30 residues cathelicidin-BF could result from a further processing.

• ·Literature 1

• • Title

  • Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics.

• • Pubmed ID

  • 18795096

• • Reference

  • PLoS One. 2008 Sep 16;3(9):e3217.

• • Author

  • Wang Y, Hong J, Liu X, Yang H, Liu R, Wu J, Wang A, Lin D, Lai R.

• ·Literature 2

• • Title

  • Identification and characterization of novel reptile cathelicidins from elapid snakes.

• • Pubmed ID

  • 18620012

• • Reference

  • Peptides. 2008 Oct;29(10):1685-1691.

• • Author

  • Zhao H, Gan TX, Liu XD, Jin Y, Lee WH, Shen JH, Zhang Y.