Reviewed, UniProtKB/Swiss-Prot P08136 (LANE_STAEP)

Names and origin

Protein names

Recommended name:
    Lantibiotic epidermin

Gene names

Name:

epiA

Encoded on

Plasmid pTu 32

Organism

Staphylococcus epidermidis

Taxonomic identifier

1282 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	52 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
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.
Sequence similarities	Belongs to the type A lantibiotic family.

Ontologies

Keywords
Molecular function	Antibiotic Antimicrobial Bacteriocin Lantibiotic
PTM	D-amino acid Thioether bond
Technical term	3D-structure Plasmid
Gene Ontology (GO)
Biological process	cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to Gram-positive bacterium Inferred from electronic annotation. Source: InterPro
Molecular function	receptor binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 30	30			PRO_0000017116
	Peptide	31 – 52	22	Lantibiotic epidermin Ref.1		PRO_0000017117
Amino acid modifications
	Modified residue	44	1	2,3-didehydrobutyrine
	Cross-link	33 ↔ 37		Lanthionine (Ser-Cys)
	Cross-link	38 ↔ 41		Beta-methyllanthionine (Thr-Cys)
	Cross-link	46 ↔ 51		Lanthionine (Ser-Cys)
	Cross-link	49 ↔ 52		S-(2-aminovinyl)-D-cysteine (Ser-Cys)

Sequences

	Sequence		Length	Mass (Da)
	P08136-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 8B1AD2875BF16D6D	FASTA	52	5,632
	10 20 30 40 50 MEAVKEKNDL FNLDVKVNAK ESNDSGAEPR IASKFICTPG CAKTGSFNSY CC

References

[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: 2835685] [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: 1740156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: TU 3298 / DSM 3095.
[3]	"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: 11101502] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 48-52 IN COMPLEX WITH EPID.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X07840 Genomic DNA. Translation: CAA30689.1.
X07840 Genomic DNA. Translation: CAA30690.1.
X62386 Genomic DNA. Translation: CAA44252.1.

PIR

EPSED. S00768.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G5Q	X-ray	2.57	M/N/O/P	48-52	[»]

ModBase

Search...

Protein family/group databases

TCDB

1.C.20.1.6. nisin family.

Family and domain databases

InterPro

IPR006078. Gallidermin.
IPR006079. Lan.
[Graphical view]

Pfam

PF02052. Gallidermin. 1 hit.
[Graphical view]

PRINTS

PR00323. GALLIDERMIN.

ProtoNet

Search...

Other Resources

PMAP-CutDB

P08136.

Entry information

Entry name

LANE_STAEP

Accession

Primary (citable) accession number: P08136
Secondary accession number(s): Q54093

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	September 1, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)