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Protein

Lantibiotic epidermin

Gene

epiA

Organism
Staphylococcus epidermidis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriocin, Lantibiotic

Protein family/group databases

TCDBi1.C.20.1.6. the nisin (nisin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Lantibiotic epidermin
Gene namesi
Name:epiA
Encoded oniPlasmid pTu 320 Publication
OrganismiStaphylococcus epidermidis
Taxonomic identifieri1282 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 30301 PublicationPRO_0000017116Add
BLAST
Peptidei31 – 5222Lantibiotic epidermin1 PublicationPRO_0000017117Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki33 ↔ 37Lanthionine (Ser-Cys)
Cross-linki38 ↔ 41Beta-methyllanthionine (Thr-Cys)
Modified residuei44 – 441(Z)-2,3-didehydrobutyrine
Cross-linki46 ↔ 51Lanthionine (Ser-Cys)
Cross-linki49 ↔ 52S-(2-aminovinyl)-D-cysteine (Ser-Cys)

Post-translational modificationi

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.
The 2,3-didehydrobutyrine is determined to be the Z-isomer.1 Publication

Keywords - PTMi

D-amino acid, Thioether bond

Miscellaneous databases

PMAP-CutDBP08136.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5QX-ray2.57M/N/O/P48-52[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08136.

Family & Domainsi

Sequence similaritiesi

Belongs to the type A lantibiotic family.Curated

Family and domain databases

InterProiIPR006079. Lantibiotic_typ-A_Bacillales.
[Graphical view]
PfamiPF02052. Gallidermin. 1 hit.
[Graphical view]
PRINTSiPR00323. GALLIDERMIN.
TIGRFAMsiTIGR03731. lantibio_gallid. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08136-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAVKEKNDL FNLDVKVNAK ESNDSGAEPR IASKFICTPG CAKTGSFNSY

CC
Length:52
Mass (Da):5,632
Last modified:August 1, 1988 - v1
Checksum:i8B1AD2875BF16D6D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07840 Genomic DNA. Translation: CAA30689.1.
X07840 Genomic DNA. Translation: CAA30690.1.
X62386 Genomic DNA. Translation: CAA44252.1.
PIRiS00768. EPSED.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07840 Genomic DNA. Translation: CAA30689.1.
X07840 Genomic DNA. Translation: CAA30690.1.
X62386 Genomic DNA. Translation: CAA44252.1.
PIRiS00768. EPSED.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5QX-ray2.57M/N/O/P48-52[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi1.C.20.1.6. the nisin (nisin) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP08136.
PMAP-CutDBP08136.

Family and domain databases

InterProiIPR006079. Lantibiotic_typ-A_Bacillales.
[Graphical view]
PfamiPF02052. Gallidermin. 1 hit.
[Graphical view]
PRINTSiPR00323. GALLIDERMIN.
TIGRFAMsiTIGR03731. lantibio_gallid. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings."
    Schnell N., Entian K.-D., Schneider U., Gotz F., Zahner H., Kellner R., Jung G.
    Nature 333:276-278(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: TU 3298 / DSM 3095.
  2. "Analysis of genes involved in the biosynthesis of lantibiotic epidermin."
    Schnell N., Engelke G., Augustin J., Rosenstein R., Ungermann V., Goetz F., Entian K.-D.
    Eur. J. Biochem. 204:57-68(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: TU 3298 / DSM 3095.
  3. "Epidermin: sequencing of a heterodetic tetracyclic 21-peptide amide antibiotic."
    Allgaier H., Jung G., Werner R.G., Schneider U., Zahner H.
    Eur. J. Biochem. 160:9-22(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-52, POST-TRANSLATIONAL MODIFICATIONS.
  4. "Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed with a pentapeptide substrate."
    Blaesse M., Kupke T., Huber R., Steinbacher S.
    EMBO J. 19:6299-6310(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 48-52 IN COMPLEX WITH EPID.

Entry informationi

Entry nameiLANE_STAEP
AccessioniPrimary (citable) accession number: P08136
Secondary accession number(s): Q54093
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: March 16, 2016
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.