Bacteriocin: Lichenicidin A1
Accession: BAC196
Classification
Class: Lantibiotic (two-peptide)
Genetics
Gene: lanA1; Synonyms=lanA, licA1; OrderedLocusNames=BL05375, BLi04127
Producer and target organisms
Producer Organism: Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Gram-positive]
Taxonomy: Bacteria
FirmicutesBacillalesBacillaceaeBacillus
Target organismsUnavailable data
Description
FUNCTION:
Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually, LchA1 exhibits activity towards L.lactis HP. When combined with LchA2, it displays activity towards a broad spectrum of non-pathogenic and pathogenic Gram-positive bacteria including strains of L.monocytogenes, methicillin-resistant S.aureus, S.pneumoniae and
strains of vancomycin-resistant enterococci, but not towards E.faecium L4001 and BM4147-1. Combined LchA1 and LchA2 peptides also inhibit Bacillus sp. HIL-Y85/54728, L.lactis DPC3417 and B.halodurans C-125, which produce lantibiotics themselves. Inactivated by proteinase K and pronase E, but not by trypsin and chymotrypsin.
SUBCELLULAR LOCATION: Secreted, cell wall.
PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor (By similarity).
Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually, LchA1 exhibits activity towards L.lactis HP. When combined with LchA2, it displays activity towards a broad spectrum of non-pathogenic and pathogenic Gram-positive bacteria including strains of L.monocytogenes, methicillin-resistant S.aureus, S.pneumoniae and
strains of vancomycin-resistant enterococci, but not towards E.faecium L4001 and BM4147-1. Combined LchA1 and LchA2 peptides also inhibit Bacillus sp. HIL-Y85/54728, L.lactis DPC3417 and B.halodurans C-125, which produce lantibiotics themselves. Inactivated by proteinase K and pronase E, but not by trypsin and chymotrypsin.
SUBCELLULAR LOCATION: Secreted, cell wall.
PTM: Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor (By similarity).
Uniprot and PDB links
PDB Entry2KTN resolved by NMR
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15461803;DOI=10.1186/gb-2004-5-10-r77
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.
"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species.", Genome Biol. 5:R77.1-R77.12(2004).
PubMed=15461803;DOI=10.1186/gb-2004-5-10-r77
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.
"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species.", Genome Biol. 5:R77.1-R77.12(2004).
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15383718;DOI=10.1159/000079829
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential.", J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
PubMed=15383718;DOI=10.1159/000079829
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential.", J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
PubMed=19561184;DOI=10.1128/AEM.00730-09
Begley M., Cotter P.D., Hill C., Ross R.P.
"Identification of a novel two-peptide lantibiotic, lichenicidin, following rational genome mining for LanM proteins.", Appl. Environ. Microbiol. 75:5451-5460(2009).
PubMed=19561184;DOI=10.1128/AEM.00730-09
Begley M., Cotter P.D., Hill C., Ross R.P.
"Identification of a novel two-peptide lantibiotic, lichenicidin, following rational genome mining for LanM proteins.", Appl. Environ. Microbiol. 75:5451-5460(2009).
IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
PubMed=19707558;DOI=10.1371/journal.pone.0006788
Dischinger J., Josten M., Szekat C., Sahl H.G., Bierbaum G.
"Production of the novel two-peptide lantibiotic lichenicidin by Bacillus licheniformis DSM 13.", PLoS ONE 4:E6788-E6788(2009).
PubMed=19707558;DOI=10.1371/journal.pone.0006788
Dischinger J., Josten M., Szekat C., Sahl H.G., Bierbaum G.
"Production of the novel two-peptide lantibiotic lichenicidin by Bacillus licheniformis DSM 13.", PLoS ONE 4:E6788-E6788(2009).
3D STRUCTURE
PubMed=20578714;DOI=10.1021/bi100871b
henkarev Z.O., Finkina E.I., Nurmukhamedova E.K., Balandin S.V., Mineev K.S., Nadezhdin K.D., Yakimenko Z.A., Tagaev A.A., Temirov Y.V., Arseniev A.S., Ovchinnikova T.V.
"Isolation, structure elucidation, and synergistic antibacterial activity of a novel two-component lantibiotic lichenicidin from Bacillus licheniformis VK21.", Biochemistry 49: 6462-6472 (2010).
PubMed=20578714;DOI=10.1021/bi100871b
henkarev Z.O., Finkina E.I., Nurmukhamedova E.K., Balandin S.V., Mineev K.S., Nadezhdin K.D., Yakimenko Z.A., Tagaev A.A., Temirov Y.V., Arseniev A.S., Ovchinnikova T.V.
"Isolation, structure elucidation, and synergistic antibacterial activity of a novel two-component lantibiotic lichenicidin from Bacillus licheniformis VK21.", Biochemistry 49: 6462-6472 (2010).
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Protein sequence
| ........10 ........20 ........30 ........40 | | | | TITLSTCAIL SKPLGNNGYL CTVTKECMPS CN |
Wheel representation
3D Structure
Protein sequence annotations
| Feature | Position(s) | Length | Description |
| PEPTIDE | 1↔32 | 32 | Lantibiotic lichenicidin A1 (Bysimilarity). Feature identifier = PRO_0000399039.
|
| Modified residue | 1 | 2-oxobutanoic acid (By similarity). | |
| Modified residue | 5 | 2,3-didehydroalanine (Ser) (Bysimilarity). | |
| Modified residue | 6 | (Z)-2,3-didehydrobutyrine (Bysimilarity). | |
| Cross-link | 3↔7 | 5 | Beta-methyllanthionine (Thr-Cys) (Bysimilarity). |
| Cross-link | 11↔21 | 11 | Lanthionine (Ser-Cys) (By similarity). |
| Cross-link | 22↔27 | 6 | Beta-methyllanthionine (Thr-Cys) (Bysimilarity). |
| Cross-link | 24↔31 | 8 | Beta-methyllanthionine (Thr-Cys) (Bysimilarity). |
Composition
Hydrophobicity
Composition
| Formula | C0
H0
N0
O0
S0 |
| Absent amino acids | DFHQRW |
| Common amino acids | T |
| Mass (Da) | 3 |
| Net charge | +1 |
| Isoelectric point | 7.91 |
| Basic residues | 2 |
| Acidic residues | 1 |
| Hydrophobic residues | 8 |
| Polar residues | 18 |
| Aliphatic residues | 7 |
| Tiny residues | 6 |
| Boman Index | -16.3 |
| Hydropathy Index | 0.284 |
| Aliphatic Index | 85.31 |
| Instability Index | 64.74 (unstable) |
| Half Life |
Mammalian : 7.2 hour Yeast : >20 hour E. coli : >10 hour |
| Extinction Coefficient | 1740 M-1 cm-1 |
| Absorbance 280nm | 56.13 |
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