ID   LAN2A_RUMFL             Reviewed;          63 AA.
AC   P0DQL3;
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=Lantipeptide Flvbeta.a {ECO:0000303|PubMed:27028884};
DE   Flags: Precursor;
GN   Name=FlvA2.a {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-30; THR-33; THR-38; THR-39; THR-54 AND THR-55, AND LANTHIONINE
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 that does probably not show
CC       antibacterial activity, since its analog [+3]Flvbeta.a does not show
CC       antibacterial activity against M.luteus (PubMed:27028884). Also does
CC       not show antibiotic activity when tested with [Del2]Flvalpha.a, an
CC       analog of Flvalpha.a, which is encoded by the same operon than
CC       Flvbeta.a (PubMed:27028884). The bactericidal activity of lantibiotics
CC       is based on depolarization of energized bacterial cytoplasmic
CC       membranes, initiated by the formation of aqueous transmembrane pores
CC       (By similarity). {ECO:0000250|UniProtKB:P86475,
CC       ECO:0000269|PubMed:27028884}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: Maturation of FlvA2 peptides involves the enzymatic conversion of
CC       Thr, and Ser into dehydrated AA and the formation of thioether bonds
CC       with cysteines (PubMed:27028884). Modifications are processed by the
CC       flavecin synthetase FlvM2 (PubMed:27028884). This is followed by
CC       membrane translocation and cleavage of the modified precursor (By
CC       similarity). {ECO:0000250|UniProtKB:H2A7G5,
CC       ECO:0000269|PubMed:27028884}.
CC   -!- PTM: Contains DL-lanthionine, when coepressed in E.coli with the
CC       flavecin synthetase FlvM2. {ECO:0000269|PubMed:27028884}.
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DR   AlphaFoldDB; P0DQL3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   3: Inferred from homology;
KW   Secreted; Thioether bond.
FT   PROPEP          1..28
FT                   /note="Cleaved by FlvT"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT                   /id="PRO_0000450396"
FT   PEPTIDE         29..63
FT                   /note="Lantipeptide Flvbeta.a"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT                   /id="PRO_0000450397"
FT   MOD_RES         30
FT                   /note="2,3-didehydrobutyrine; by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   MOD_RES         33
FT                   /note="2,3-didehydrobutyrine; by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   MOD_RES         38
FT                   /note="2,3-didehydrobutyrine; by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   MOD_RES         39
FT                   /note="2,3-didehydrobutyrine; by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   MOD_RES         54
FT                   /note="2,3-didehydrobutyrine; by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   MOD_RES         55
FT                   /note="2,3-didehydrobutyrine; by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   CROSSLNK        43..49
FT                   /note="Lanthionine (Ser-Cys); by FlvM2"
FT                   /evidence="ECO:0000305|PubMed:27028884"
SQ   SEQUENCE   63 AA;  6800 MW;  4B9C9DFC2284C6F9 CRC64;
     MSEKNMEKAG VVKADELDEM IDETTGGAST VNTVGIHTTY LISKGLQNCP LKPTTILPIL
     PRK