ID   LAN1A_RUMFL             Reviewed;          80 AA.
AC   P0DQM1;
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 Flvalpha.a {ECO:0000303|PubMed:27028884};
DE   Flags: Precursor;
GN   Name=FlvA1.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-43 AND THR-47, AND LANTHIONINE AND METHYLLANTHIONINE 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) only
CC       active on Gram-positive bacteria in synergy with Flvbeta peptides,
CC       which are encoded by the same operon than Flvalpha.a (PubMed:27028884).
CC       Shows antibacterial activity in synergy with Flvbeta.b, Flvbeta.c,
CC       Flvbeta.e and Flvbeta.g (PubMed:27028884). Does not show antibacterial
CC       activity when tested with Flvbeta.a, Flvbeta.d, Flvbeta.f and Flvbeta.h
CC       (PubMed:27028884). The bactericidal activity of lantibiotics is based
CC       on depolarization of energized bacterial cytoplasmic membranes,
CC       initiated by the formation of aqueous transmembrane pores (By
CC       similarity). {ECO:0000250|UniProtKB:P86475,
CC       ECO:0000269|PubMed:27028884}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: The lanthionine formed by Ser-58 and Cys-68 forms a putative lipid
CC       II binding motif. {ECO:0000305|PubMed:27028884}.
CC   -!- PTM: Maturation of FlvA1 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 FlvM1 (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 and DL-beta-methyllanthionine, when
CC       coepressed in E.coli with the flavecin synthetase FlvM1.
CC       {ECO:0000269|PubMed:27028884}.
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DR   AlphaFoldDB; P0DQM1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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; Lipid-binding;
KW   Secreted; Thioether bond.
FT   PROPEP          1..38
FT                   /note="Cleaved by FlvT"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT                   /id="PRO_0000450388"
FT   PEPTIDE         39..80
FT                   /note="Lantibiotic Flvalpha.a"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT                   /id="PRO_0000450389"
FT   MOD_RES         43
FT                   /note="2,3-didehydrobutyrine; by FlvM1"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   MOD_RES         47
FT                   /note="2,3-didehydrobutyrine; by FlvM1"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   CROSSLNK        52..55
FT                   /note="Beta-methyllanthionine (Thr-Cys); by FlvM1"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   CROSSLNK        58..68
FT                   /note="Lanthionine (Ser-Cys); by FlvM1"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   CROSSLNK        69..74
FT                   /note="Beta-methyllanthionine (Thr-Cys); by FlvM1"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT   CROSSLNK        71..78
FT                   /note="Beta-methyllanthionine (Thr-Cys); by FlvM1"
FT                   /evidence="ECO:0000305|PubMed:27028884"
SQ   SEQUENCE   80 AA;  8458 MW;  C1E580DDD6E439CE CRC64;
     MNKNPIYRSE EEAKDIACGN VAAELDENSQ ALDAINGAGW KQTIVCTIAQ GTVGCLVSYG
     LGNGGYCCTY TVECSKTCNK