• • 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

• • Biological Activity

  • Antimicrobial, Antibacterial, Anti-Gram+

• • Target Organism

  • • [Ref.17213266] MICs between 1 and 12.5 mg/L: 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: Escherichia coli ATCC 8739, Pseudomonas aeruginosa ATCC 9027, S. gordonii Challis ATCC 49818 and Staphylococcus aureus ATCC 6538.
    • MICs over 100mg/L: 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.

• • Helical Wheel Diagram

  • 

• • 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.