• DRAMP ID

    • DRAMP00216
    • Peptide Name

    • Antimicrobial peptide LCI (Bacteriocin)
    • Source

    • Bacillus subtilis (Gram-positive bacteria)
    • Family

    • Not found
    • Gene

    • Not found
    • Sequence

    • AIKLVQSPNGNFAASFVLDGTKWIFKSKYYDSSKGYWVGIYEVWDRK
    • Sequence Length

    • 47
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial
    • Target Organism

    • X. oryzae pv oryzae, R. solanacearum.
    • Hemolytic Activity

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

      • Not included yet
    • Binding Target

    • DNA or mRNA
    • 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

    • Beta strand (4 strands; 27 residues)
    • Structure Description

    • The solution structure of LCI has a novel topology, containing a four-strand antiparallel beta-sheet as the dominant secondary structure.
    • Helical Wheel Diagram

    • DRAMP00216 helical wheel diagram
    • PDB ID

    • 2B9K resolved by NMR.
  • 2B9K-> 
    • Predicted Structure

    • There is no predicted structure for DRAMP00216.
    • Formula

    • C259H378N62O69
    • Absent Amino Acids

    • CHM
    • Common Amino Acids

    • K
    • Mass

    • 5464.22
    • PI

    • 9.4
    • Basic Residues

    • 7
    • Acidic Residues

    • 4
    • Hydrophobic Residues

    • 18
    • Net Charge

    • +3
    • Boman Index

    • -54.26
    • Hydrophobicity

    • -0.351
    • Aliphatic Index

    • 72.55
    • Half Life

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

    • 22460
    • Absorbance 280nm

    • 488.26
    • Polar Residues

    • 16

DRAMP00216

DRAMP00216 chydropathy plot
    • Function

    • Has antibacterial activity against X.oryzae pv oryzae and R.solanacearum. May bind DNA or mRNA.
    • Miscellaneous

    • Heat stable. Resistant to proteolysis by tryspin and pepsin, but susceptible to pronase E and proteinase K.
  • ·Literature 1
    • Title

    • Characterization of an anti-rice bacterial blight polypeptide LCI.
    • Reference

    • Rice Genet. Newsl. 1990;7:151-154.
    • Author

    • Liu JY, Pan NS, Chen ZL.
  • ·Literature 2
    • Title

    • Solution structure of LCI, an AMP from Bacillus subtilis.
    • Reference

    • iochemistry. 2011 May 10;50(18):3621-3627.
    • Author

    • Xia, B, Gong, W, Lu, G.