LAN2E_RUMFL
ID LAN2E_RUMFL Reviewed; 72 AA.
AC P0DQL7;
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.e {ECO:0000303|PubMed:27028884};
DE Flags: Precursor;
GN Name=FlvA2.e {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 SER-37; THR-48 AND THR-49, 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 active on Gram-positive bacteria, since its analog
CC [Del1]Flvbeta.e shows antibacterial activity against Gram-positive
CC bacteria (PubMed:27028884). This activity is not synergistically
CC enhanced by [Del2]Flvalpha.a, an analog of Flvalpha.a, which is encoded
CC by the same operon than Flvbeta.e (PubMed:27028884). The bactericidal
CC activity of lantibiotics is based on depolarization of energized
CC bacterial 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; P0DQL7; -.
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_0000450404"
FT PEPTIDE 35..72
FT /note="Lantibiotic Flvbeta.e"
FT /evidence="ECO:0000305|PubMed:27028884"
FT /id="PRO_0000450405"
FT MOD_RES 37
FT /note="2,3-didehydroalanine (Ser); 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 MOD_RES 49
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; 7751 MW; 1D4D4716707C4E73 CRC64;
MNNKEFNMEQ FKKLAAVVSE DELDEMLDEN VTGAASSIPC AKVVVKVTTV VVAATTGFDW
CPTGACTTSC RF