Bacteriocin: lacticin 3147 A1
Accession: BAC039
Classification
Class: Lantibiotic
Genetics
Gene: ltnA1; Synonyms=ltnA; ORFNames=ORF00035
Producer and target organisms
Producer Organism: Lactococcus lactis subsp (Streptococcus lactis), lactis [Gram-positive]
Taxonomy: Bacteria
FirmicutesLactobacillalesStreptococcaceaeLactococcus
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 A1 exhibits strong activity towards L.lactis strain AM2, weak activity towards L.lactis strain HP and no activity towards L.lactis strain IFPL359, but when combined with lacticin 3147 A2 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.
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 A1 exhibits strong activity towards L.lactis strain AM2, weak activity towards L.lactis strain HP and no activity towards L.lactis strain IFPL359, but when combined with lacticin 3147 A2 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: O87236
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).
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).
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).
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).
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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Gene structure
| Gene id | Name | Description | Location |
| BACGene141 | ORF00037 | lacticin 481/lactococcin biosynthesis protein LCNDR2 similar to SP:P37609 PID:433322 percent identity: 28.41; identified by sequencesimilarity; putative | 28174..31116 |
| BACGene142 | ORF00039 | lacticin 481/lactococcin biosynthesis protein LCNDR2 similar to SP:P37609 PID:433322 percent identity: 27.01; identified by sequencesimilarity; putative | 33357..36140 |
Protein sequence
| ........10 ........20 ........30 ........40 | | | | CSTNTFSLSD YWGNNGAWCT LTHECMAWCK |
Wheel representation
Protein sequence annotations
| Feature | Position(s) | Length | Description |
| PEPTIDE | 1↔30 | 30 | Lantibiotic lacticin 3147 A1. Feature identifier = PRO_0000042850. |
| Modified residue | 3 | 2,3-didehydrobutyrine. | |
| Modified residue | 5 | 2,3-didehydrobutyrine. | |
| Modified residue | 7 | 2,3-didehydroalanine (Ser). | |
| Cross-link | 1↔2 | 2 | Lanthionine (Cys-Ser). |
| Cross-link | 9↔19 | 11 | Lanthionine (Ser-Cys). |
| Cross-link | 20↔25 | 6 | Beta-methyllanthionine (Thr-Cys). |
| Cross-link | 22↔29 | 8 | Beta-methyllanthionine (Thr-Cys). |
Composition
Hydrophobicity
Composition
| Formula | C148
H209
N39
O46
S5 |
| Absent amino acids | IPQRV |
| Common amino acids | CT |
| Mass (Da) | 3449.32 |
| Net charge | 0 |
| Isoelectric point | 5.44 |
| Basic residues | 2 |
| Acidic residues | 2 |
| Hydrophobic residues | 8 |
| Polar residues | 17 |
| Aliphatic residues | 2 |
| Tiny residues | 7 |
| Boman Index | -33.5 |
| Hydropathy Index | -0.29 |
| Aliphatic Index | 32.67 |
| Instability Index | 28.85 (stable) |
| Half Life |
Mammalian : 1.2 hour Yeast : >20 hour E. coli : >10 hour |
| Extinction Coefficient | 18240 M-1 cm-1 |
| Absorbance 280nm | 628.97 |
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