Bacteriocin: Lichenicidin A2

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Bacteriocin: Lichenicidin A2

Accession: BAC197

Classification
Genetics
Gene: lanA2; Synonyms=licA2; OrderedLocusNames=BLi04126.1, BL05375.1
Producer and target organisms

Producer Organism: Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Gram-positive]

Taxonomy: BacteriaFirmicutesBacillalesBacillaceaeBacillus

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, LchA2 exhibits activity towards L.lactis HP. When combined with LchA1, 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

UniProt Entry: P86720

PDB Entry2KTO 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).
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).
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).
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).
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).
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Protein sequence
 ........10 ........20 ........30 ........40 
          |          |          |          | 
 TTPATTSSWT CITAGVTVSA SLCPTTKCTS RC

Wheel representation
wheel representation of Lichenicidin A2
3D Structure
Protein sequence annotations
Features of Lichenicidin A2

TTTTSTTT
FeaturePosition(s)LengthDescription
PEPTIDE1↔3232
Lantibiotic lichenicidin A2 (Bysimilarity).
Feature identifier = PRO_0000399041.
Modified residue12-oxobutanoic acid (By similarity).
Modified residue2(Z)-2,3-didehydrobutyrine (Bysimilarity).
Modified residue5(Z)-2,3-didehydrobutyrine (Bysimilarity).
Modified residue6(Z)-2,3-didehydrobutyrine (Bysimilarity).
Modified residue82,3-didehydroalanine (Ser) (Bysimilarity).
Modified residue13(Z)-2,3-didehydrobutyrine (Bysimilarity).
Modified residue17(Z)-2,3-didehydrobutyrine (Bysimilarity).
Modified residue26(Z)-2,3-didehydrobutyrine (Bysimilarity).
Cross-link7↔115Lanthionine (Ser-Cys) (By similarity).
Cross-link19↔235Lanthionine (Ser-Cys) (By similarity).
Cross-link25↔284Beta-methyllanthionine (Thr-Cys) (Bysimilarity).
Cross-link29↔324Beta-methyllanthionine (Thr-Cys) (Bysimilarity).
Composition
Hydrophobicity

Composition
Formula C0 H0 N0 O0 S0
Absent amino acids DEFHMNQY
Common amino acids T
Mass (Da) 3
Net charge +2
Isoelectric point 8.34
Basic residues 2
Acidic residues 0
Hydrophobic residues 8
Polar residues 20
Aliphatic residues 4
Tiny residues 9
Boman Index -31.43
Hydropathy Index 0.256
Aliphatic Index 51.88
Instability Index 36.6 (stable)
Half Life Mammalian : 7.2 hour
Yeast : >20 hour
E. coli : >10 hour
Extinction Coefficient 5750 M-1 cm-1
Absorbance 280nm 185.48

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