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P36504 (DURA_STRGV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lantibiotic duramycin
Alternative name(s):
Antibiotic PA48009
Leucopeptin
OrganismStreptoverticillium griseoverticillatum
Taxonomic identifier68215 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces cinnamoneus group

Protein attributes

Sequence length19 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is a potent inhibitor of human phospholipase A2. Ref.2

Subcellular location

Secreted Probable Ref.2.

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 or the formation of dialkylamine bonds with lysine. This is followed by membrane translocation and cleavage of the modified precursor.

Sequence similarities

Belongs to the type B lantibiotic family.

Mass spectrometry

Molecular mass is 2014 Da from positions 1 - 19. Determined by FAB. Ref.2

Ontologies

Keywords
   Cellular componentSecreted
   Molecular functionAntibiotic
Antimicrobial
Bacteriocin
Lantibiotic
   PTMHydroxylation
Thioether bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Peptide1 – 1919Lantibiotic duramycin
PRO_0000043970

Amino acid modifications

Modified residue151(3R)-3-hydroxyaspartate
Cross-link1 ↔ 18Beta-methyllanthionine (Cys-Thr)
Cross-link4 ↔ 14Lanthionine (Ser-Cys)
Cross-link5 ↔ 11Beta-methyllanthionine (Cys-Thr)
Cross-link6 ↔ 19Lysinoalanine (Ser-Lys)

Sequences

Sequence LengthMass (Da)Tools
P36504 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 012951AE27362F00

FASTA192,069
        10 
CKQSCSFGPF TFVCDGNTK 

« Hide

References

[1]"The structure of PA48009: the revised structure of duramycin."
Hayashi F., Nagashima K., Terui Y., Kawamura Y., Matsumoto K., Itazaki H.
J. Antibiot. 43:1421-1430(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, STRUCTURE BY NMR.
Strain: PA-48009.
[2]"Duramycins B and C, two new lanthionine containing antibiotics as inhibitors of phospholipase A2. Structural revision of duramycin and cinnamycin."
Fredenhagen A., Fendrich G., Marki F., Marki W., Gruner J., Raschdorf F., Peter H.H.
J. Antibiot. 43:1403-1412(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, CROSS-LINKS, HYDROXYLATION AT ASP-15, SUBCELLULAR LOCATION.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameDURA_STRGV
AccessionPrimary (citable) accession number: P36504
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 14, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families