LANLB_BACLI
ID LANLB_BACLI Reviewed; 72 AA.
AC P86476; E0YCK0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Lantibiotic lichenicidin VK21 A2 {ECO:0000303|PubMed:20578714};
DE Short=LchA2 {ECO:0000303|PubMed:20578714};
DE Flags: Precursor;
GN Name=lchA2 {ECO:0000303|PubMed:20578714};
OS Bacillus licheniformis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 41-72, FUNCTION,
RP MASS SPECTROMETRY, STRUCTURE BY NMR OF 41-72, OXOBUTANOIC ACID FORMATION AT
RP THR-41, DEHYDRATION AT THR-42; THR-45; THR-46; SER-48; THR-53; THR-57 AND
RP THR-66, AND LANTHIONINE CROSS-LINKS.
RC STRAIN=VK21 {ECO:0000269|PubMed:20578714};
RX PubMed=20578714; DOI=10.1021/bi100871b;
RA Shenkarev Z.O., Finkina E.I., Nurmukhamedova E.K., Balandin S.V.,
RA Mineev K.S., Nadezhdin K.D., Yakimenko Z.A., Tagaev A.A., Temirov Y.V.,
RA Arseniev A.S., Ovchinnikova T.V.;
RT "Isolation, structure elucidation, and synergistic antibacterial activity
RT of a novel two-component lantibiotic Lichenicidin from Bacillus
RT licheniformis VK21.";
RL Biochemistry 49:6462-6472(2010).
CC -!- FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic)
CC active on Gram-positive bacteria. 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. When present individually, LchA2 exhibits activity
CC towards B.subtilis L1 (IC(50)=30 uM), Rhodococcus sp. SS2 (IC(50)=16.6
CC uM), M.luteus B1314 (IC(50)=2.6 uM), B.megaterium VKM41 (IC(50)=2 uM),
CC S.aureus 209p (IC(50)=20 uM), B.pumilus 2001, B.globigii I,
CC B.amyloliquefaciens I, M.smegmatis 1171 and M.phlei 1291. However, when
CC combined with LchA1, it displays much stronger activity against
CC B.subtilis L1 (IC(50)=0.64 uM), Rhodococcus sp. SS2 (IC(50)=0.64 uM),
CC M.luteus B1314 (IC(50)=0.09 uM), B.megaterium VKM41 (IC(50)=0.12 uM)
CC and S.aureus 209p (IC(50)=0.64 uM). The activity of the combined LchA1
CC and LchA2 peptides is strongest at a molar ratio of 1. Even when
CC applied at 17-fold concentration of the highest IC(50) values for Gram-
CC positive bacteria, neither the individual nor the combined peptides
CC display activity against Gram-negative bacteria P.aeruginosa PAO1,
CC P.putida I-97 or E.coli C600. {ECO:0000269|PubMed:20578714}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20578714,
CC ECO:0000305}.
CC -!- PTM: Maturation of lantibiotics involves the enzymatic conversion of
CC Thr, and Ser into dehydrated AA and the formation of thioether bonds
CC with cysteine. This is followed by membrane translocation and cleavage
CC of the modified precursor. {ECO:0000250|UniProtKB:O87237,
CC ECO:0000269|PubMed:20578714}.
CC -!- PTM: The 2,3-didehydrobutyrines are determined to be the Z-isomers.
CC {ECO:0000269|PubMed:20578714}.
CC -!- MASS SPECTROMETRY: Mass=3019.36; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:20578714};
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DR EMBL; GU949560; ADM36017.1; -; Genomic_DNA.
DR RefSeq; WP_003186379.1; NZ_VTQZ01000003.1.
DR PDB; 2KTO; NMR; -; A=42-72.
DR PDBsum; 2KTO; -.
DR AlphaFoldDB; P86476; -.
DR SMR; P86476; -.
DR GeneID; 66213936; -.
DR PATRIC; fig|1402.63.peg.4090; -.
DR EvolutionaryTrace; P86476; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR InterPro; IPR027632; Lant_SP_1948.
DR Pfam; PF16934; Mersacidin; 1.
DR TIGRFAMs; TIGR03893; lant_SP_1948; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin;
KW Direct protein sequencing; Lantibiotic; Secreted; Thioether bond.
FT PROPEP 1..40
FT /evidence="ECO:0000269|PubMed:20578714"
FT /id="PRO_0000399044"
FT PEPTIDE 41..72
FT /note="Lantibiotic lichenicidin VK21 A2"
FT /evidence="ECO:0000269|PubMed:20578714"
FT /id="PRO_0000399045"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="2-oxobutanoic acid"
FT /evidence="ECO:0000269|PubMed:20578714"
FT MOD_RES 42
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:20578714"
FT MOD_RES 45
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:20578714"
FT MOD_RES 46
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:20578714"
FT MOD_RES 48
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000269|PubMed:20578714"
FT MOD_RES 53
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:20578714"
FT MOD_RES 57
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:20578714"
FT MOD_RES 66
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:20578714"
FT CROSSLNK 47..51
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000269|PubMed:20578714"
FT CROSSLNK 59..63
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000269|PubMed:20578714"
FT CROSSLNK 65..68
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:20578714"
FT CROSSLNK 69..72
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:20578714"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:2KTO"
SQ SEQUENCE 72 AA; 7448 MW; 83D1B85F650E0123 CRC64;
MKTMKNSAAR EAFKGANHPA GMVSEEELKA LVGGNDVNPE TTPATTSSWT CITAGVTVSA
SLCPTTKCTS RC
