ID   DURC_STRGP              Reviewed;          19 AA.
AC   P36503;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Lantibiotic duramycin C;
OS   Streptomyces griseoluteus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=29306;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, CROSS-LINKS, HYDROXYLATION
RP   AT ASP-15, AND SUBCELLULAR LOCATION.
RC   STRAIN=R2107;
RX   PubMed=2125590; DOI=10.7164/antibiotics.43.1403;
RA   Fredenhagen A., Fendrich G., Marki F., Marki W., Gruner J., Raschdorf F.,
RA   Peter H.H.;
RT   "Duramycins B and C, two new lanthionine containing antibiotics as
RT   inhibitors of phospholipase A2. Structural revision of duramycin and
RT   cinnamycin.";
RL   J. Antibiot. 43:1403-1412(1990).
RN   [2]
RP   STRUCTURE BY NMR.
RC   STRAIN=R2107;
RA   Zimmermann N., Freund S., Fredenhagen A., Jung G.;
RT   "Solution structure of the lantibiotics duramycin B and C.";
RL   (In) Schneider C.H., Eberles A.N. (eds.);
RL   Peptides 1992, pp.519-520, Escom Science Publishers, Leiden (1993).
RN   [3]
RP   STRUCTURE BY NMR, MASS SPECTROMETRY, CROSS-LINKS, HYDROXYLATION AT ASP-15,
RP   CONFIGURATION OF STEREOCENTERS, AND SUBCELLULAR LOCATION.
RC   STRAIN=R2107;
RX   PubMed=8375380; DOI=10.1111/j.1432-1033.1993.tb18159.x;
RA   Zimmermann N., Freund S., Fredenhagen A., Jung G.;
RT   "Solution structures of the lantibiotics duramycin B and C.";
RL   Eur. J. Biochem. 216:419-428(1993).
CC   -!- FUNCTION: Is a potent inhibitor of human phospholipase A2. Exhibits
CC       only a weak antibacterial activity against B.subtilis, and does not
CC       display antimicrobial activity against S.aureus, S.mitis, E.coli,
CC       K.pneumoniae, P.vulgaris and C.albicans. {ECO:0000269|PubMed:2125590}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:2125590,
CC       ECO:0000305|PubMed:8375380}.
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 or the formation of dialkylamine bonds with lysine. This
CC       is followed by membrane translocation and cleavage of the modified
CC       precursor.
CC   -!- MASS SPECTROMETRY: Mass=1951; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:2125590};
CC   -!- MASS SPECTROMETRY: Mass=1950.0; Mass_error=0.8; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8375380};
CC   -!- SIMILARITY: Belongs to the type B lantibiotic family. {ECO:0000305}.
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DR   AlphaFoldDB; P36503; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW   Hydroxylation; Lantibiotic; Secreted; Thioether bond.
FT   PEPTIDE         1..19
FT                   /note="Lantibiotic duramycin C"
FT                   /id="PRO_0000043972"
FT   MOD_RES         15
FT                   /note="(3R)-3-hydroxyaspartate"
FT                   /evidence="ECO:0000269|PubMed:2125590,
FT                   ECO:0000269|PubMed:8375380"
FT   CROSSLNK        1..18
FT                   /note="Beta-methyllanthionine (Cys-Thr)"
FT   CROSSLNK        4..14
FT                   /note="Lanthionine (Ser-Cys)"
FT   CROSSLNK        5..11
FT                   /note="Beta-methyllanthionine (Cys-Thr)"
FT   CROSSLNK        6..19
FT                   /note="Lysinoalanine (Ser-Lys)"
SQ   SEQUENCE   19 AA;  2007 MW;  E2404ECE3F95286A CRC64;
     CANSCSYGPL TWSCDGNTK