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P36504

- DURA_STRGV

UniProt

P36504 - DURA_STRGV

Protein

Lantibiotic duramycin

Gene
N/A
Organism
Streptoverticillium griseoverticillatum
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Is a potent inhibitor of human phospholipase A2.1 Publication

    GO - Biological processi

    1. cytolysis Source: UniProtKB-KW
    2. defense response to bacterium Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Bacteriocin, Lantibiotic

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lantibiotic duramycin
    Alternative name(s):
    Antibiotic PA48009
    Leucopeptin
    OrganismiStreptoverticillium griseoverticillatum
    Taxonomic identifieri68215 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces cinnamoneus group

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Peptidei1 – 1919Lantibiotic duramycinPRO_0000043970Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki1 ↔ 18Beta-methyllanthionine (Cys-Thr)
    Cross-linki4 ↔ 14Lanthionine (Ser-Cys)
    Cross-linki5 ↔ 11Beta-methyllanthionine (Cys-Thr)
    Cross-linki6 ↔ 19Lysinoalanine (Ser-Lys)
    Modified residuei15 – 151(3R)-3-hydroxyaspartate1 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 or the formation of dialkylamine bonds with lysine. This is followed by membrane translocation and cleavage of the modified precursor.

    Keywords - PTMi

    Hydroxylation, Thioether bond

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the type B lantibiotic family.Curated

    Sequencei

    Sequence statusi: Complete.

    P36504-1 [UniParc]FASTAAdd to Basket

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    CKQSCSFGPF TFVCDGNTK                                     19
    Length:19
    Mass (Da):2,069
    Last modified:June 1, 1994 - v1
    Checksum:i012951AE27362F00
    GO

    Mass spectrometryi

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

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiDURA_STRGV
    AccessioniPrimary (citable) accession number: P36504
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 37 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3