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1.C.20.1.6
Class I lantibiotic bacteriocin, Epidermin precursor (has a mersacidin-like Lipid II domain, and forms Lipid II-dependent pores) (Sahl & Bierbaum, 2008).  The genetic organization, biosynthesis, modification, excretion, extracellular activation of the modified pre-peptide by proteolytic processing, self-protection of the producer, gene regulation, structure, and mode of actionhave been reviewed (Götz et al. 2014).

Accession Number:P08136
Protein Name:LANE aka EPIA
Length:52
Molecular Weight:5632.00
Species:Staphylococcus epidermidis [1282]
Location1 / Topology2 / Orientation3: Secreted1
Substrate small molecules, electrolytes, water

Cross database links:

Pfam: PF02052   

Gene Ontology

GO:0005102 F:receptor binding
GO:0019835 P:cytolysis
GO:0050830 P:defense response to Gram-positive bacterium

References (3)

[1] “Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings.”  Schnell N.et.al.   2835685
[2] “Analysis of genes involved in the biosynthesis of lantibiotic epidermin.”  Schnell N.et.al.   1740156
[3] “Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed with a pentapeptide substrate.”  Blaesse M.et.al.   11101502
Structure:
1G5Q     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MEAVKEKNDL FNLDVKVNAK ESNDSGAEPR IASKFICTPG CAKTGSFNSY CC