View bacteriocin : Epidermin

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Accession BAC017
Name Epidermin
Gene epiA
Class Lantibiotic
Producer Organism Staphylococcus epidermidis [Gram-positive]
Taxonomy BacteriaFirmicutesBacillalesStaphylococcus
Target organisms active on Gram-positive bacteria
Swiss-Prot Entry P08136 Q54093
PDB Entry 1G5Q resolved by X-ray
Other databases EMBL X07840EMBL X07840EMBL X62386EMBL A12927PIR S00768

InterPro IPR006078InterPro IPR006079Pfam PF02052PRINTS PR00323
Description Mode of action:
Lanthionine-containing peptide antibiotic (lantibiotic). The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.

Post-translational modification:
Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. The C-terminal lanthionine undergoes decarboxylation. This is followed by membrane translocation and cleavage of the modified precursor.
[Ref. 1] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=TU 3298 / DSM 3095
MEDLINE=88216821;PubMed=2835685;DOI=10.1038/333276a0
Schnell N., Entian K.-D., Schneider U., Gotz F., Zahner H., Kellner R., Jung G.
"Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings.", Nature 333:276-278(1988).

[Ref. 2] | View abstract | Export citation
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=TU 3298 / DSM 3095
MEDLINE=92155237;PubMed=1740156;
Schnell N., Engelke G., Augustin J., Rosenstein R., Ungermann V., Goetz F., Entian K.-D.
"Analysis of genes involved in the biosynthesis of lantibiotic epidermin.", Eur. J. Biochem. 204:57-68(1992).

[Ref. 3] | View abstract | Export citation
X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 48-52 IN COMPLEX WITH EPID.
MEDLINE=20553209;PubMed=11101502;DOI=10.1093/emboj/19.23.6299
Blaesse M., Kupke T., Huber R., Steinbacher S.
"Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed with a pentapeptide substrate.", EMBO J. 19:6299-6310(2000).

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Sequence
 ........10 ........20 ........30 
          |          |          | 
 IASKFICTPG CAKTGSFNSY CC
Wheel representation
Structure
Composition
Formula C99 H153 N25 O30 S4
Absent amino acids DEHLMQRVW
Common amino acids C
Mass (Da) 2320.05
Net charge +2
Isoelectric point 8.33
Basic residues 2
Acidic residues 0
Hydrophobic residues 6
Polar residues 13
Aliphatic residues 2
Tiny residues 7
Boman Index -6.8
Hydropathy Index 0.43
Aliphatic Index 44.55
Instability Index 20.5 (stable)
Half Life Mammalian : 20 hour
Yeast : 30 min
E. coli : >10 hour
Extinction Coefficient 1740 M-1 cm-1
Absorbance 280nm 82.86
Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).


Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).


Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.

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