ID   LAN2G_RUMFL             Reviewed;          72 AA.
AC   P0DQL9;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Lantibiotic Flvbeta.g {ECO:0000303|PubMed:27028884};
DE   Flags: Precursor;
GN   Name=FlvA2.g {ECO:0000303|PubMed:27028884};
OS   Ruminococcus flavefaciens.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], EXPRESSION IN E.COLI, DEHYDRATION AT
RP   THR-37; THR-46 AND THR-48, AND LANTHIONINE AND METHYLLANTHIONINE
RP   CROSS-LINKS.
RC   STRAIN=FD-1;
RX   PubMed=27028884; DOI=10.1016/j.chembiol.2015.11.014;
RA   Zhao X., van der Donk W.A.;
RT   "Structural characterization and bioactivity analysis of the two-component
RT   lantibiotic Flv system from a ruminant bacterium.";
RL   Cell Chem. Biol. 23:246-256(2016).
CC   -!- FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic) that
CC       is probably weakly active on Gram-positive bacteria, since its analog
CC       [Del1]Flvbeta.g shows weak antibacterial activity against M.luteus
CC       (PubMed:27028884). This activity is synergistically enhanced by
CC       [Del2]Flvalpha.a, an analog of Flvalpha.a, which is encoded by the same
CC       operon than Flvbeta.g (PubMed:27028884). 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 (By similarity). {ECO:0000250|UniProtKB:P86475,
CC       ECO:0000269|PubMed:27028884}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: Contains LL-lanthionine and DL-beta-methyllanthionine, when
CC       coepressed in E.coli with the flavecin synthetase FlvM2.
CC       {ECO:0000269|PubMed:27028884}.
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DR   AlphaFoldDB; P0DQL9; -.
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   3: Inferred from homology;
KW   Antibiotic; Antimicrobial; Bacteriocin; Lantibiotic; Secreted;
KW   Thioether bond.
FT   PROPEP          1..34
FT                   /note="Cleaved by FlvT"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT                   /id="PRO_0000450408"
FT   PEPTIDE         35..72
FT                   /note="Lantibiotic Flvbeta.g"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT                   /id="PRO_0000450409"
FT   MOD_RES         37
FT                   /note="2,3-didehydrobutyrine; by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   MOD_RES         46
FT                   /note="2,3-didehydrobutyrine; by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   MOD_RES         48
FT                   /note="2,3-didehydrobutyrine; by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   CROSSLNK        36..40
FT                   /note="Lanthionine (Ser-Cys); by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   CROSSLNK        55..61
FT                   /note="Beta-methyllanthionine (Thr-Cys); by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   CROSSLNK        63..66
FT                   /note="Beta-methyllanthionine (Thr-Cys); by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   CROSSLNK        67..70
FT                   /note="Beta-methyllanthionine (Thr-Cys); by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
SQ   SEQUENCE   72 AA;  7731 MW;  A6A2B2D1DAB91BF5 CRC64;
     MNNNNFDMEK FKKLAAIVSE GEIDEMLDET TVGAASTLPC AEVVVTVTGI IVKATTGFDW
     CPTGACTHSC RF