DURB_STRGW
ID DURB_STRGW Reviewed; 19 AA.
AC P36502;
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 B;
OS Streptomyces sp. (strain R2075) (Streptoverticillium sp. (strain R2075)).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=35759;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, CROSS-LINKS, HYDROXYLATION
RP AT ASP-15, AND SUBCELLULAR LOCATION.
RC STRAIN=R2075;
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=R2075;
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=R2075;
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=2008; Method=FAB;
CC Evidence={ECO:0000269|PubMed:2125590};
CC -!- MASS SPECTROMETRY: Mass=2006.7; Mass_error=0.4; 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; P36502; -.
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 B"
FT /id="PRO_0000043971"
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; 2063 MW; 0133445E27362F00 CRC64;
CRQSCSFGPL TFVCDGNTK