Bacteriocin: epidermin
Accession: BAC017
Classification
Class: Lantibiotic
Genetics
Gene: epiA
Producer and target organisms
Producer Organism: Staphylococcus epidermidis [Gram-positive]
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.
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.
Uniprot and PDB links
PDB Entry1G5Q resolved by X-ray
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).
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).
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).
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).
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).
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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Gene structure
Gene id | Name | Description | Location |
BACGene30 | epiY' | none of previously described start codons for Staphylococci (ATG,TTg,GTG) is present | complement(1..827) |
BACGene31 | epiY | none of previously described start codons for Staphylococci (ATG,TTg,GTG) is present | complement(781..1227) |
BACGene32 | epiA | Epidermin prepeptide | 1381..1539 |
BACGene33 | epiB | modifying enzyme | 1605..4565 |
BACGene34 | epiC | modifying enzyme | 4441..5808 |
BACGene35 | epiD | modifying enzyme | 5824..6369 |
BACGene36 | epiQ | response regulator | complement(6366..6983) |
BACGene37 | epiP | serine protease | complement(6994..8379) |
Protein sequence
........10 ........20 ........30 | | | IASKFICTPG CAKTGSFNSY CC |
Wheel representation
3D Structure
Protein sequence annotations
Feature | Position(s) | Length | Description |
PEPTIDE | 1↔22 | 22 | Lantibiotic epidermin. Feature identifier = PRO_0000017117. |
Modified residue | 14 | (Z)-2,3-didehydrobutyrine. | |
Cross-link | 3↔7 | 5 | Lanthionine (Ser-Cys). |
Cross-link | 8↔11 | 4 | Beta-methyllanthionine (Thr-Cys). |
Cross-link | 16↔21 | 6 | Lanthionine (Ser-Cys). |
Cross-link | 19↔22 | 4 | S-(2-aminovinyl)-D-cysteine (Ser-Cys). |
Composition
Hydrophobicity
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 |
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