General Information

    • DRAMP ID

    • DRAMP18225

    • Peptide Name

    • Subtilosin A1 (Bacteriocin)

    • Source

    • Bacillus subtilis

    • Family

    • Belongs to the class I bacteriocin

    • Gene

    • Not found

    • Sequence

    • NKGCAICSIGAACLVDGPIPDFEIAGATGLFGLWG

    • Sequence Length

    • 35

    • UniProt Entry

    • No entry found

    • Protein Existence

Activity Information

    • Biological Activity

    • Antimicrobial, Antibacterial

    • Target Organism

      • [Ref.19633086]Gram-postive bacterium:Bacillus subtilis(MIC= 250μM), Bacillus anthracis(MIC= 16μM), Bacillus cereus(MIC= 40μM), Bacillus thuringiensis(MIC= 40μM), Enterococcus faecalis(MIC= 100μM), taphylococcus carnosus(MIC= 100μM), Listeria monocytogenes(MIC= 40μM), Streptococcus pyogenes (MIC= 100μM).

    • Hemolytic Activity

      • [Ref.19633086] MLC=16 μM against rabbit blood agar

    • Cytotoxicity

    • No cytotoxicity information found in the reference(s) presented

    • Binding Target

    • Not found

Structure Information

    • Linear/Cyclic

    • Cyclic

    • N-terminal Modification

    • No specific N-terminal

    • C-terminal Modification

    • No specific C-terminal

    • Nonterminal Modifications and Unusual Amino Acids

    • Thioether bridges between Cys4 and Phe31,Cys7 and Thr28,Cys13 and Phe22.

    • Stereochemistry

    • Mixed(D-Thr28,D-Phe31)

    • Structure

    • Not found

    • Structure Description

    • A variant of Subtilosin A, where residue T6 in Subtilosin A has been mutated to isoleucine. Like Subtilosin A, it is an N- and C-circulated peptide with three rare cross-links between the sulfurs of Cys13, Cys7, and Cys 4 and the alpha-carbons of Phe22, THr28, and Phe31, respectively.

    • Helical Wheel Diagram

    • DRAMP18225 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP18225.

Physicochemical Information

    • Formula

    • C154H238N38O45S3

    • Absent Amino Acids

    • HMQRY

    • Common Amino Acids

    • G

    • Mass

    • 3437.99

    • PI

    • 4.03

    • Basic Residues

    • 1

    • Acidic Residues

    • 3

    • Hydrophobic Residues

    • 16

    • Net Charge

    • -2

    • Boman Index

    • 2383

    • Hydrophobicity

    • 0.84

    • Aliphatic Index

    • 100.57

    • Half Life

      • Mammalian:1.4 hour
      • Yeast:3 min
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 5625

    • Absorbance 280nm

    • 165.44

    • Polar Residues

    • 13

DRAMP18225

DRAMP18225 chydropathy plot

Comments Information

    • Fuction

    • Active against B. anthracis, B. cereus, B. thuringiensis, E. faecalis, S. carnosus, L. monocytogenes, and S. pyogenes. In addition to the hemolytic activity, subtilosin A1 was found to exhibit enhanced antimicrobial activity against specific bacterial strains.

Literature Information

  • ·Literature 1

    • Title

    • Isolation of a variant of subtilosin A with hemolytic activity.

    • Reference

    • J Bacteriol. 2009 Sep;191(18):5690-6.

    • Author

    • Huang T, Geng H, Miyyapuram VR, Sit CS, Vederas JC, Nakano MM.