Bacteriocin: lacticin 3147 A2

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Bacteriocin: lacticin 3147 A2

Accession: BAC038

Classification
Class: Lantibiotic
Genetics
Gene: ltnA2; Synonyms=ltnB; ORFNames=ORF00036
Producer and target organisms

Producer Organism: Lactococcus lactis subsp (Streptococcus lactis), lactis [Gram-positive]

Taxonomy: BacteriaFirmicutesLactobacillalesStreptococcaceaeLactococcus

Target organismsactive on Gram-positive bacteria: Enterococcus - Lactobacillus - Lactococcus - Leuconostoc

Description
Mode of action:
Lanthionine-containing peptide antibiotic (lantibiotic). 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 lacticin 3147 A2 exhibits weak activity towards L.lactis strain AM2 and L.lactis strain HP, and no activity towards L.lactis strain IFPL359, but when combined with lacticin 3147 A1 it displays strong activity towards all three strains.

Post-translational modification:
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. NOTE=Ref.2. NOTE=Ref.3. NOTE=Ref.4.
Uniprot and PDB links

UniProt Entry: O87237

PDB EntryUnknown

NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=DPC3147; PLASMID=pMRC01
MEDLINE=99000510;PubMed=9767571;
Dougherty B.A., Hill C., Weidman J.F., Richardson D.R., Venter J.C., Ross R.P.
"Sequence and analysis of the 60 kb conjugative, bacteriocin-producing plasmid pMRC01 from Lactococcus lactis DPC3147.", Mol. Microbiol. 29:1029-1038(1998).
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 51-57, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY, STRAIN=IFPL105; PLASMID=pBAC105
MEDLINE=20430196;PubMed=10971756;DOI=10.1046/j.1365-2672.2000.01103.x
Martinez-Cuesta M.C., Buist G., Kok J., Hauge H.H., Nissen-Meyer J., Pelaez C., Requena T.
"Biological and molecular characterization of a two-peptide lantibiotic produced by Lactococcus lactis IFPL105.", J. Appl. Microbiol. 89:249-260(2000).
PROTEIN SEQUENCE OF 37-65, MASS SPECTROMETRY, AND THIOETHER BONDS, STRAIN=DPC3147
PubMed=15023056;DOI=10.1021/bi0362065
Martin N.I., Sprules T., Carpenter M.R., Cotter P.D., Hill C., Ross R.P., Vederas J.C.
"Structural characterization of lacticin 3147, a two-peptide lantibiotic with synergistic activity.", Biochemistry 43:3049-3056(2004).
FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY, STRAIN=DPC3147
MEDLINE=20076413;PubMed=10608807;DOI=10.1074/jbc.274.53.37544
Ryan M.P., Jack R.W., Josten M., Sahl H.-G., Jung G., Ross R.P., Hill C.
"Extensive post-translational modification, including serine to D- alanine conversion, in the two-component lantibiotic, lacticin 3147.", J. Biol. Chem. 274:37544-37550(1999).
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End Note
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Gene structure
genome of lacticin 3147 A2

Gene idNameDescriptionLocation
BACGene139ORF00037lacticin 481/lactococcin biosynthesis protein LCNDR2 similar to SP:P37609 PID:433322 percent identity: 28.41; identified by sequencesimilarity; putative28174..31116
BACGene140ORF00039lacticin 481/lactococcin biosynthesis protein LCNDR2 similar to SP:P37609 PID:433322 percent identity: 27.01; identified by sequencesimilarity; putative33357..36140
ORF00037ORF00039
Protein sequence
 ........10 ........20 ........30 
          |          |          | 
 TTPATPAISI LSAYISTNTC PTTKCTRAC

Wheel representation
wheel representation of lacticin 3147 A2
Protein sequence annotations
Features of lacticin 3147 A2

TTTSS
FeaturePosition(s)LengthDescription
PEPTIDE1↔2929
Lantibiotic lacticin 3147 A2.
Feature identifier = PRO_0000042852.
Modified residue12-oxobutanoic acid.
Modified residue22,3-didehydrobutyrine.
Modified residue52,3-didehydrobutyrine.
Modified residue92,3-didehydroalanine (Ser).
Modified residue122,3-didehydroalanine (Ser).
Cross-link16↔205Lanthionine (Ser-Cys).
Cross-link22↔254Beta-methyllanthionine (Thr-Cys).
Cross-link26↔294Beta-methyllanthionine (Thr-Cys).
Composition
Hydrophobicity

Composition
Formula C126 H212 N34 O43 S3
Absent amino acids DEFGHMQVW
Common amino acids T
Mass (Da) 3005.92
Net charge +2
Isoelectric point 8.51
Basic residues 2
Acidic residues 0
Hydrophobic residues 8
Polar residues 16
Aliphatic residues 4
Tiny residues 7
Boman Index -27.25
Hydropathy Index 0.21
Aliphatic Index 67.59
Instability Index 54.5 (unstable)
Half Life Mammalian : 7.2 hour
Yeast : >20 hour
E. coli : >10 hour
Extinction Coefficient 1615 M-1 cm-1
Absorbance 280nm 57.68

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