ID   LAN1B_RUMFL             Reviewed;          80 AA.
AC   P0DQM2;
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.b {ECO:0000303|PubMed:27028884};
DE   Flags: Precursor;
GN   Name=FlvA1.B {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].
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. Shows
CC       antibacterial activity in synergy with Flvbeta.b, Flvbeta.c, Flvbeta.e
CC       and Flvbeta.g. Does not show antibacterial activity when tested with
CC       Flvbeta.a, Flvbeta.d, Flvbeta.f and Flvbeta.h (By similarity). The
CC       bactericidal activity of lantibiotics is based on depolarization of
CC       energized bacterial cytoplasmic membranes, initiated by the formation
CC       of aqueous transmembrane pores (By similarity).
CC       {ECO:0000250|UniProtKB:P0DQM1, ECO:0000250|UniProtKB:P86475}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DQM1}.
CC   -!- PTM: The lanthionine formed by Ser-58 and Cys-68 forms a putative lipid
CC       II binding motif. {ECO:0000250|UniProtKB:P0DQM1}.
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. Modifications are processed by the flavecin synthetase
CC       FlvM1 (By similarity). This is followed by membrane translocation and
CC       cleavage of the modified precursor (By similarity).
CC       {ECO:0000250|UniProtKB:H2A7G5, ECO:0000250|UniProtKB:P0DQM1}.
CC   -!- PTM: Contains DL-lanthionine and DL-beta-methyllanthionine, when
CC       coepressed in E.coli with the flavecin synthetase FlvM1.
CC       {ECO:0000250|UniProtKB:P0DQM1}.
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DR   AlphaFoldDB; P0DQM2; -.
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_0000450390"
FT   PEPTIDE         39..80
FT                   /note="Lantibiotic Flvalpha.b"
FT                   /evidence="ECO:0000305|PubMed:27028884"
FT                   /id="PRO_0000450391"
FT   MOD_RES         43
FT                   /note="2,3-didehydrobutyrine; by FlvM1"
FT                   /evidence="ECO:0000250|UniProtKB:P0DQM1"
FT   MOD_RES         47
FT                   /note="2,3-didehydrobutyrine; by FlvM1"
FT                   /evidence="ECO:0000250|UniProtKB:P0DQM1"
FT   CROSSLNK        52..55
FT                   /note="Beta-methyllanthionine (Thr-Cys); by FlvM1"
FT                   /evidence="ECO:0000250|UniProtKB:P0DQM1"
FT   CROSSLNK        58..68
FT                   /note="Lanthionine (Ser-Cys); by FlvM1"
FT                   /evidence="ECO:0000250|UniProtKB:P0DQM1"
FT   CROSSLNK        69..74
FT                   /note="Beta-methyllanthionine (Thr-Cys); by FlvM1"
FT                   /evidence="ECO:0000250|UniProtKB:P0DQM1"
FT   CROSSLNK        71..78
FT                   /note="Beta-methyllanthionine (Thr-Cys); by FlvM1"
FT                   /evidence="ECO:0000250|UniProtKB:P0DQM1"
SQ   SEQUENCE   80 AA;  8458 MW;  C1EB6E3DD80AD9CE CRC64;
     MNKNPIYRSE EEAKNIACGN VAAELDENSQ ALDAINGAGW KQTIVCTIAQ GTVGCLVSYG
     LGNGGYCCTY TVECSKTCNK