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Protein

Lantibiotic actagardine

Gene
N/A
Organism
Actinoplanes liguriensis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Has antibacterial activity against some Gram-positive bacteria. Has good antistreptococcal activity.

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriocin, Lantibiotic

Names & Taxonomyi

Protein namesi
Recommended name:
Lantibiotic actagardine
Alternative name(s):
Gardimycin
OrganismiActinoplanes liguriensis
Taxonomic identifieri69484 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicromonosporalesMicromonosporaceaeActinoplanes

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Peptidei1 – 1919Lantibiotic actagardinePRO_0000043967Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki1 ↔ 6Lanthionine (Ser-Cys)1 Publication
Cross-linki7 ↔ 12Beta-methyllanthionine (Thr-Cys)1 Publication
Cross-linki9 ↔ 17Beta-methyllanthionine (Thr-Cys)1 Publication
Cross-linki14 ↔ 19Beta-methyllanthionine sulfoxide (Thr-Cys)

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. The 14-19 beta-methyllanthionine thioether bond is oxidized to a sulfoxide. This is followed by membrane translocation and cleavage of the modified precursor.

Keywords - PTMi

Oxidation, Thioether bond

Structurei

Secondary structure

1
19
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ1NMR-A2-19[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56650.

Family & Domainsi

Sequence similaritiesi

Belongs to the type B lantibiotic family.Curated

Sequencei

Sequence statusi: Complete.

P56650-1 [UniParc]FASTAAdd to basket

« Hide

        10 
SSGWVCTLTI ECGTVICAC
Length:19
Mass (Da):1,946
Last modified:November 8, 2002 - v2
Checksum:i5C138C7CEE8765B3
GO

Sequence databases

PIRiA58700.

Cross-referencesi

Sequence databases

PIRiA58700.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ1NMR-A2-19[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP56650.

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "Sequence determination of actagardine, a novel lantibiotic, by homonuclear 2D NMR spectroscopy."
    Kettenring J.K., Malabarba A., Vekey K., Cavalleri B.
    J. Antibiot. 43:1082-1088(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE, STRUCTURE BY NMR.
  2. "The tetracyclic lantibiotic actagardine. 1H-NMR and 13C-NMR assignments and revised primary structure."
    Zimmermann N., Metzger J.W., Jung G.
    Eur. J. Biochem. 228:786-797(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, STRUCTURE BY NMR.
  3. "The three-dimensional solution structure of the lantibiotic murein-biosynthesis-inhibitor actagardine determined by NMR."
    Zimmermann N., Jung G.
    Eur. J. Biochem. 246:809-819(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiLANA_ACTLG
AccessioniPrimary (citable) accession number: P56650
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 8, 2002
Last modified: June 24, 2015
This is version 46 of the entry and version 2 of the sequence. [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
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.