• • DRAMP ID

  • DRAMP00169

• • Peptide Name

  • Enterocin AS-48 (AS-48; Bacteriocin)

• • Source

  • Enterococcus faecalis S-48 (Gram-positive bacteria)

• • Family

  • Belongs to the class IIc bacteriocin

• • Gene

  • as-48

• • Sequence

  • MAKEFGIPAAVAGTVINVVEAGGWVTTIVSILTAVGSGGLSLLAAAGRESIKAYLKKEIKKKGKRAVIAW

• • Sequence Length

  • 70

• • UniProt Entry

  • Q47765

• • Protein Existence

  • Protein level

• • Biological Activity

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

• • Target Organism

  • • Gram-positive bacteria: Bacillus subtilus, Bacillus cereus, Bacillus circulans, Bacillus megaterium, Corynebacterium glutamicum, Corynebacterium bovis, Mycobacterium phlei, Nocardia corrallina, Micrococcus luteus, Micrococcus lysodeikticus, Staphylococcus aureus, Streptococcus faecalis, Streptococcus faecium;
    • Gram-negative bacteria: Enterobacter cloacae, Escherichia coli, Klebsiella pneumoniae, Proteus inconstans, Salmonella typhimurium, Shigella sonnei, Pseudomonas fluorescens, Pseudomonas aeruginosa, Pseudomonas reptilivora.

• • 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

  • Cell membrane

• • Linear/Cyclic

  • Cyclic

• • N-terminal Modification

  • No specific N-terminal

• • C-terminal Modification

  • No specific C-terminal

• • Nonterminal Modifications and Unusual Amino Acids

  • Hydrogen bonds between Ala-2 and Ile-7, Val-18 and Gly-23, Thr-33 and Gly-36, the backbone carbonyl oxygen of Phe-5 and the side-chain hydroxylic proton of Ser-50

• • Stereochemistry

  • L

• • Structure

  • Alpha helix (6 helices; 54 residues)

• • Structure Description

  • The NMR structure of AS-48 at pH 3 showed that AS-48 is a monomer consisting of a bundle of five helices arranged with the topology of the saposin fold.

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 1E68 resolved by NMR. 1O82,1O83,1O84 resolved by X-ray.

• Predicted Structure

• There is no predicted structure for DRAMP00169.

DRAMP00169

• • Function

  • The bacteriocin AS-48 is a membrane-interacting peptide, which displays a broad anti-microbial spectrum against Gram-positive and Gram-negative bacteria. The antimicrobial effect of AS-48 is due to its ability to form pores in the membranes of sensitive bacteria, leading to the efflux of small molecules and the depletion of the membrane electrical potential and ultimately leading to cell death.

• ·Literature 1

• • Title

  • Bactericidal and bacteriolytic action of peptide antibiotic AS-48 against gram-positive and Gram-negative bacteria and other organisms.

• • Pubmed ID

  • 2501837

• • Reference

  • Res Microbiol. 1989 Jan;140(1):57-68.

• • Author

  • G¡lvez A, Maqueda M, Mart­nez-Bueno M, Valdivia E.

• ·Literature 2

• • Title

  • Structure of bacteriocin AS-48: from soluble state to membrane bound state.

• • Pubmed ID

  • 14623193

• • Reference

  • J Mol Biol. 2003 Nov 28;334(3):541-549.

• • Author

  • S¡nchez-Barrena MJ, Mart­nez-Ripoll M, G¡lvez A, Valdivia E, Maqueda M, Cruz V, Albert A.

• ·Literature 3

• • Title

  • Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin.

• • Pubmed ID

  • 11005847

• • Reference

  • Proc Natl Acad Sci U S A. 2000 Oct 10;97(21):11221-6.

• • Author

  • Gonz¡lez C, Langdon GM, Bruix M, G¡lvez A, Valdivia E, Maqueda M, Rico M.