LANE_STAEP
ID LANE_STAEP Reviewed; 52 AA.
AC P08136; Q54093;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Lantibiotic epidermin;
DE Flags: Precursor;
GN Name=epiA;
OS Staphylococcus epidermidis.
OG Plasmid pTu 32.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TU 3298 / DSM 3095;
RX PubMed=2835685; DOI=10.1038/333276a0;
RA Schnell N., Entian K.-D., Schneider U., Gotz F., Zahner H., Kellner R.,
RA Jung G.;
RT "Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic
RT with four sulphide-rings.";
RL Nature 333:276-278(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TU 3298 / DSM 3095;
RX PubMed=1740156; DOI=10.1111/j.1432-1033.1992.tb16605.x;
RA Schnell N., Engelke G., Augustin J., Rosenstein R., Ungermann V., Goetz F.,
RA Entian K.-D.;
RT "Analysis of genes involved in the biosynthesis of lantibiotic epidermin.";
RL Eur. J. Biochem. 204:57-68(1992).
RN [3]
RP PROTEIN SEQUENCE OF 31-52, DEHYDRATION AT THR-44, AND LANTHIONINE
RP CROSS-LINKS.
RX PubMed=3769923; DOI=10.1111/j.1432-1033.1986.tb09933.x;
RA Allgaier H., Jung G., Werner R.G., Schneider U., Zahner H.;
RT "Epidermin: sequencing of a heterodetic tetracyclic 21-peptide amide
RT antibiotic.";
RL Eur. J. Biochem. 160:9-22(1986).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 48-52 IN COMPLEX WITH EPID.
RX PubMed=11101502; DOI=10.1093/emboj/19.23.6299;
RA Blaesse M., Kupke T., Huber R., Steinbacher S.;
RT "Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed
RT with a pentapeptide substrate.";
RL EMBO J. 19:6299-6310(2000).
CC -!- FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic)
CC active on Gram-positive bacteria. The bactericidal activity of
CC lantibiotics is based on depolarization of energized bacterial
CC cytoplasmic membranes, initiated by the formation of aqueous
CC transmembrane pores.
CC -!- PTM: Maturation of lantibiotics involves the enzymatic conversion of
CC Thr, and Ser into dehydrated AA and the formation of thioether bonds
CC with cysteine. The C-terminal lanthionine undergoes decarboxylation.
CC This is followed by membrane translocation and cleavage of the modified
CC precursor.
CC -!- PTM: The 2,3-didehydrobutyrine is determined to be the Z-isomer.
CC {ECO:0000269|PubMed:3769923}.
CC -!- SIMILARITY: Belongs to the type A lantibiotic family. {ECO:0000305}.
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DR EMBL; X07840; CAA30689.1; -; Genomic_DNA.
DR EMBL; X07840; CAA30690.1; -; Genomic_DNA.
DR EMBL; X62386; CAA44252.1; -; Genomic_DNA.
DR PIR; S00768; EPSED.
DR RefSeq; WP_002498697.1; NZ_CZRO020000143.1.
DR PDB; 1G5Q; X-ray; 2.57 A; M/N/O/P=48-52.
DR PDBsum; 1G5Q; -.
DR AlphaFoldDB; P08136; -.
DR SMR; P08136; -.
DR TCDB; 1.C.20.1.6; the nisin (nisin) family.
DR EvolutionaryTrace; P08136; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR006079; Lantibiotic_typ-A_Bacillales.
DR Pfam; PF02052; Gallidermin; 1.
DR PRINTS; PR00323; GALLIDERMIN.
DR TIGRFAMs; TIGR03731; lantibio_gallid; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin; D-amino acid;
KW Direct protein sequencing; Lantibiotic; Plasmid; Thioether bond.
FT PROPEP 1..30
FT /evidence="ECO:0000269|PubMed:3769923"
FT /id="PRO_0000017116"
FT PEPTIDE 31..52
FT /note="Lantibiotic epidermin"
FT /evidence="ECO:0000269|PubMed:2835685"
FT /id="PRO_0000017117"
FT MOD_RES 44
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:3769923"
FT CROSSLNK 33..37
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000269|PubMed:3769923"
FT CROSSLNK 38..41
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:3769923"
FT CROSSLNK 46..51
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000269|PubMed:3769923"
FT CROSSLNK 49..52
FT /note="S-(2-aminovinyl)-D-cysteine (Ser-Cys)"
FT /evidence="ECO:0000269|PubMed:3769923"
SQ SEQUENCE 52 AA; 5632 MW; 8B1AD2875BF16D6D CRC64;
MEAVKEKNDL FNLDVKVNAK ESNDSGAEPR IASKFICTPG CAKTGSFNSY CC