• • DRAMP ID

  • DRAMP00167

• • Peptide Name

  • Subtilosin A (Antilisterial bacteriocin subtilosin; D-amino acid; Bacteriocin; Preclinical)

• • Source

  • Bacillus subtilis (strain 168) (Gram-positive bacteria)

• • Family

  • Belongs to the class IIc bacteriocin

• • Gene

  • sboA

• • Sequence

  • NKGCATCSIGAACLVDGPIPDFEIAGATGLFGLWG

• • Sequence Length

  • 35

• • UniProt Entry

  • O07623

• • Protein Existence

  • Protein level

• • SMILES

  • Not available

• • Biological Activity

  • Antimicrobial, Antibacterial, Anti-Gram+

• • Target Organism

  • • [Ref.17213266] MICs between 1 and 12.5 mg/L:

      Target Organism	Activity
      E. faecalis OGX-1	-
      L. monocytogenes ATCC 19115	-
      P. gingivalis ATCC 33277	-
      K. rhizophila ATCC 9341	-
      Enterobacter aerogenes ATCC 13408	-
      Streptococcus pyogenes ATCC 19615 and Shigella sonnei ATCC 25931	-

    • MICs between 25 and 100 mg/L:

      Target Organism	Activity
      Escherichia coli ATCC 8739	-
      Pseudomonas aeruginosa ATCC 9027	-
      S. gordonii Challis ATCC 49818 and Staphylococcus aureus ATCC 6538	-

    • MICs over 100mg/L:

      Target Organism	Activity
      B. subtilis ATCC 6633	-
      Fusobacterium nucleatum ATCC 25586	-
      P. gingivalis W83	-
      K. pneumoniae ATCC 4352	-
      K. pneumoniae UMN1	-
      Bacillus cereus ATCC 10876	-
      Staphylococcus epidermidis ATCC 12228	-
      Proteus mirabilis ATCC 25933	-
      Salmonella enterica Typhi ATCC 12048	-

• • Hemolytic Activity

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

• • Cytotoxicity

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

• • Binding Target

  • Not found

• • 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

  • Alpha helix (1 helices; 6 residues)

• • Structure Description

  • The NMR study results demonstrate that in addition to having a cyclized peptide backbone (amide between N and C termini), three cross-links are formed between the sulfurs of Cys13, Cys7, and Cys4 and the alpha-positions of Phe22, Thr28, and Phe31, respectively.

• • PDB ID

  • 1PXQ resolved by NMR.

• Predicted Structure

• There is no predicted structure for DRAMP00167.

DRAMP00167

• • PTM

  • This peptide undergoes unique processing steps that include proteolytic cleavage after Glu-8, and covalent linkage of the alpha-amino of Asn-9 with the carboxyl of Gly-43 to form a cyclopeptide. Thioether cross-links are formed between cysteines and the alpha-carbons of other amino acids, Cys-12 to Phe-39, Cys- 15 to Thr-36, and Cys-21 to Phe-30. In forming these cross-links, Thr-36 and Phe-39 are converted to D-amino-acids. and 39 probably due to their modification, and reports a cyclic permutation of the peptide sequence.

• ·Literature 1

• • Title

  • Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis.

• • Pubmed ID

  • 3936839

• • Reference

  • J Biochem. 1985 Sep;98(3):585-603.

• • Author

  • Babasaki K, Takao T, Shimonishi Y, Kurahashi K.

• ·Literature 2

• • Title

  • Structure of subtilosin A, a cyclic antimicrobial peptide from Bacillus subtilis with unusual sulfur to alpha-carbon cross-links: formation and reduction of alpha-thio-alpha-amino acid derivatives.

• • Pubmed ID

  • 15035610

• • Reference

  • Biochemistry. 2004 Mar 30;43(12):3385-3395.

• • Author

  • Kawulka KE, Sprules T, Diaper CM, Whittal RM, McKay RT, Mercier P, Zuber P, Vederas JC.