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Protein

Lantibiotic lichenicidin VK21 A2

Gene

lchA2

Organism
Bacillus licheniformis
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, LchA2 exhibits activity towards B.subtilis L1 (IC50=30 µM), Rhodococcus sp. SS2 (IC50=16.6 µM), M.luteus B1314 (IC50=2.6 µM), B.megaterium VKM41 (IC50=2 µM), S.aureus 209p (IC50=20 µM), B.pumilus 2001, B.globigii I, B.amyloliquefaciens I, M.smegmatis 1171 and M.phlei 1291. However, when combined with LchA1, it displays much stronger activity against B.subtilis L1 (IC50=0.64 µM), Rhodococcus sp. SS2 (IC50=0.64 µM), M.luteus B1314 (IC50=0.09 µM), B.megaterium VKM41 (IC50=0.12 µM) and S.aureus 209p (IC50=0.64 µM). The activity of the combined LchA1 and LchA2 peptides is strongest at a molar ratio of 1. Even when applied at 17-fold concentration of the highest IC50 values for Gram-positive bacteria, neither the individual nor the combined peptides display activity against Gram-negative bacteria P.aeruginosa PAO1, P.putida I-97 or E.coli C600.1 Publication

GO - Molecular functioni

GO - Biological processi

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

Keywordsi

Molecular functionAntibiotic, Antimicrobial, Bacteriocin, Lantibiotic

Names & Taxonomyi

Protein namesi
Recommended name:
Lantibiotic lichenicidin VK21 A21 Publication
Short name:
LchA21 Publication
Gene namesi
Name:lchA21 Publication
OrganismiBacillus licheniformis
Taxonomic identifieri1402 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: UniProtKB

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00003990441 – 401 PublicationAdd BLAST40
PeptideiPRO_000039904541 – 72Lantibiotic lichenicidin VK21 A2Add BLAST32

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei412-oxobutanoic acid1 Publication1
Modified residuei42(Z)-2,3-didehydrobutyrine1 Publication1
Modified residuei45(Z)-2,3-didehydrobutyrine1 Publication1
Modified residuei46(Z)-2,3-didehydrobutyrine1 Publication1
Cross-linki47 ↔ 51Lanthionine (Ser-Cys)1 Publication
Modified residuei482,3-didehydroalanine (Ser)1 Publication1
Modified residuei53(Z)-2,3-didehydrobutyrine1 Publication1
Modified residuei57(Z)-2,3-didehydrobutyrine1 Publication1
Cross-linki59 ↔ 63Lanthionine (Ser-Cys)1 Publication
Cross-linki65 ↔ 68Beta-methyllanthionine (Thr-Cys)1 Publication
Modified residuei66(Z)-2,3-didehydrobutyrine1 Publication1
Cross-linki69 ↔ 72Beta-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.By similarity1 Publication
The 2,3-didehydrobutyrines are determined to be the Z-isomers.1 Publication

Keywords - PTMi

Thioether bond

Proteomic databases

PRIDEiP86476

Interactioni

GO - Molecular functioni

Structurei

Secondary structure

172
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi59 – 62Combined sources4

3D structure databases

SMRiP86476
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP86476

Family & Domainsi

Family and domain databases

InterProiView protein in InterPro
IPR027632 Lant_SP_1948
PfamiView protein in Pfam
PF16934 Mersacidin, 1 hit
TIGRFAMsiTIGR03893 lant_SP_1948, 1 hit

Sequencei

Sequence statusi: Complete.

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

P86476-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTMKNSAAR EAFKGANHPA GMVSEEELKA LVGGNDVNPE TTPATTSSWT
60 70
CITAGVTVSA SLCPTTKCTS RC
Length:72
Mass (Da):7,448
Last modified:May 3, 2011 - v2
Checksum:i83D1B85F650E0123
GO

Mass spectrometryi

Molecular mass is 3019.36 Da from positions 41 - 72. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GU949560 Genomic DNA Translation: ADM36017.1
RefSeqiWP_003186379.1, NZ_PVZQ01000002.1

Genome annotation databases

GeneIDi23673978
PATRICifig|1402.63.peg.4090

Similar proteinsi

Entry informationi

Entry nameiLANLB_BACLI
AccessioniPrimary (citable) accession number: P86476
Secondary accession number(s): E0YCK0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: May 3, 2011
Last modified: July 18, 2018
This is version 26 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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