ID   DURA_STRGV              Reviewed;          19 AA.
AC   P36504;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Lantibiotic duramycin;
DE   AltName: Full=Antibiotic PA48009;
DE   AltName: Full=Leucopeptin;
OS   Streptomyces griseoverticillatus (Streptoverticillium griseoverticillatum).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces cinnamoneus group.
OX   NCBI_TaxID=68215;
RN   [1]
RP   PROTEIN SEQUENCE, AND STRUCTURE BY NMR.
RC   STRAIN=PA-48009;
RX   PubMed=2272918; DOI=10.7164/antibiotics.43.1421;
RA   Hayashi F., Nagashima K., Terui Y., Kawamura Y., Matsumoto K., Itazaki H.;
RT   "The structure of PA48009: the revised structure of duramycin.";
RL   J. Antibiot. 43:1421-1430(1990).
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, CROSS-LINKS, HYDROXYLATION
RP   AT ASP-15, AND SUBCELLULAR LOCATION.
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).
CC   -!- FUNCTION: Is a potent inhibitor of human phospholipase A2.
CC       {ECO:0000269|PubMed:2125590}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:2125590}.
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=2014; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:2125590};
CC   -!- SIMILARITY: Belongs to the type B lantibiotic family. {ECO:0000305}.
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DR   AlphaFoldDB; P36504; -.
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.
DR   InterPro; IPR046016; DUF5973.
DR   Pfam; PF19398; DUF5973; 1.
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"
FT                   /id="PRO_0000043970"
FT   MOD_RES         15
FT                   /note="(3R)-3-hydroxyaspartate"
FT                   /evidence="ECO:0000269|PubMed:2125590"
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;  2069 MW;  012951AE27362F00 CRC64;
     CKQSCSFGPF TFVCDGNTK