LANLA_BACLI
ID LANLA_BACLI Reviewed; 74 AA.
AC P86475; E0YCK1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Lantibiotic lichenicidin VK21 A1 {ECO:0000303|PubMed:20578714};
DE Short=LchA1 {ECO:0000303|PubMed:20578714};
DE Flags: Precursor;
GN Name=lchA1 {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 43-74, FUNCTION,
RP MASS SPECTROMETRY, STRUCTURE BY NMR OF 43-74, OXOBUTANOIC ACID FORMATION AT
RP THR-43, DEHYDRATION AT SER-47 AND THR-48, 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, LchA1 exhibits activity
CC towards B.subtilis L1 (IC(50)=9 uM), Rhodococcus sp. SS2 (IC(50)=9 uM),
CC M.luteus B1314 (IC(50)=1.2 uM), B.megaterium VKM41 (IC(50)=1.8 uM),
CC S.aureus 209p (IC(50)=3.1 uM), B.pumilus 2001, B.globigii I,
CC B.amyloliquefaciens I, M.smegmatis 1171 and M.phlei 1291. However, when
CC combined with LchA2, 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:O87236,
CC ECO:0000269|PubMed:20578714}.
CC -!- PTM: The 2,3-didehydrobutyrine is determined to be the Z-isomer.
CC {ECO:0000269|PubMed:20578714}.
CC -!- MASS SPECTROMETRY: Mass=3249.51; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:20578714};
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DR EMBL; GU949560; ADM36018.1; -; Genomic_DNA.
DR RefSeq; WP_003186381.1; NZ_VTQZ01000003.1.
DR PDB; 2KTN; NMR; -; A=44-74.
DR PDBsum; 2KTN; -.
DR AlphaFoldDB; P86475; -.
DR SMR; P86475; -.
DR GeneID; 66213935; -.
DR PATRIC; fig|1402.62.peg.575; -.
DR EvolutionaryTrace; P86475; -.
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; IPR029243; Lantibiotic_alpha.
DR Pfam; PF14867; Lantibiotic_a; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin;
KW Direct protein sequencing; Lantibiotic; Secreted; Thioether bond.
FT PROPEP 1..42
FT /evidence="ECO:0000269|PubMed:20578714"
FT /id="PRO_0000399042"
FT PEPTIDE 43..74
FT /note="Lantibiotic lichenicidin VK21 A1"
FT /evidence="ECO:0000269|PubMed:20578714"
FT /id="PRO_0000399043"
FT MOD_RES 43
FT /note="2-oxobutanoic acid"
FT /evidence="ECO:0000269|PubMed:20578714"
FT MOD_RES 47
FT /note="2,3-didehydroalanine (Ser)"
FT /evidence="ECO:0000269|PubMed:20578714"
FT MOD_RES 48
FT /note="(Z)-2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:20578714"
FT CROSSLNK 45..49
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:20578714"
FT CROSSLNK 53..63
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000269|PubMed:20578714"
FT CROSSLNK 64..69
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:20578714"
FT CROSSLNK 66..73
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:20578714"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2KTN"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2KTN"
SQ SEQUENCE 74 AA; 8208 MW; A9B07B85B9118C56 CRC64;
MSKKEMILSW KNPMYRTESS YHPAGNILKE LQEEEQHSIA GGTITLSTCA ILSKPLGNNG
YLCTVTKECM PSCN
