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Protein

Lantibiotic lacticin 3147 A2

Gene

ltnA2

Organism
Lactococcus lactis subsp. lactis (Streptococcus lactis)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 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.2 Publications

GO - Molecular functioni

GO - Biological processi

  • cytolysis Source: UniProtKB-KW
  • defense response to Gram-positive bacterium Source: UniProtKB

Keywordsi

Molecular functionAntibiotic, Antimicrobial, Bacteriocin, Lantibiotic

Protein family/group databases

TCDBi1.C.21.2.4 the lacticin 481 (lacticin 481) family

Names & Taxonomyi

Protein namesi
Recommended name:
Lantibiotic lacticin 3147 A2
Gene namesi
Name:ltnA21 Publication
Synonyms:ltnBImported
ORF Names:ORF00036
Encoded oniPlasmid pMRC01Imported
Plasmid pBAC105Imported
OrganismiLactococcus lactis subsp. lactis (Streptococcus lactis)
Taxonomic identifieri1360 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000428511 – 361 PublicationAdd BLAST36
PeptideiPRO_000004285237 – 65Lantibiotic lacticin 3147 A21 PublicationAdd BLAST29

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei372-oxobutanoic acid1 Publication1
Modified residuei382,3-didehydrobutyrine1 Publication1
Modified residuei412,3-didehydrobutyrine1 Publication1
Modified residuei452,3-didehydroalanine (Ser)1 Publication1
Modified residuei482,3-didehydroalanine (Ser)1 Publication1
Cross-linki52 ↔ 56Lanthionine (Ser-Cys)1 Publication
Cross-linki58 ↔ 61Beta-methyllanthionine (Thr-Cys)1 Publication
Cross-linki62 ↔ 65Beta-methyllanthionine (Thr-Cys)1 Publication

Post-translational modificationi

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.1 Publication
It is not established whether the 2,3-didehydrobutyrines are the E- or Z-isomers (PubMed:15023056 and PubMed:10608807). In the NMR model they were assumed to be the Z-isomer.

Keywords - PTMi

Thioether bond

Interactioni

GO - Molecular functioni

Structurei

3D structure databases

ProteinModelPortaliO87237
SMRiO87237
ModBaseiSearch...
MobiDBiSearch...

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O87237-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEKNMKKND TIELQLGKYL EDDMIELAEG DESHGGTTPA TPAISILSAY
60
ISTNTCPTTK CTRAC
Length:65
Mass (Da):7,080
Last modified:November 1, 1998 - v1
Checksum:iDD063A6B5DCE5F82
GO

Mass spectrometryi

Molecular mass is 2848 Da from positions 37 - 65. Determined by PD. 1 Publication
Molecular mass is 2847.40 Da from positions 37 - 65. Determined by MALDI. 1 Publication
Molecular mass is 2847.47 Da from positions 37 - 65. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001272 Genomic DNA Translation: AAC56054.1
AF167432 Genomic DNA Translation: AAF32257.1
PIRiT43107
RefSeqiNP_047320.1, NC_001949.1

Genome annotation databases

GeneIDi1113496

Similar proteinsi

Entry informationi

Entry nameiLANA2_LACLL
AccessioniPrimary (citable) accession number: O87237
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 1, 1998
Last modified: May 23, 2018
This is version 51 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Plasmid
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health