A0A084G2W8 · DEFS2_PSEDA

Function

function

Antibacterial peptide potently active against Gram-positive bacteria (PubMed:29174563).
May act by selectively inhibiting peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis (By similarity).
Shows remarkably activity against resistant isolates such as methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococci (VRE) at the concentration of micromolar level (PubMed:29174563).
Does not act by destroying the membrane integrity, which is consistent with its nonamphiphilic architecture (PubMed:29174563).
Acts more rapidly than vancomycin (PubMed:29174563).
Shows low hemolysis and cytotoxicity and high serum stability (PubMed:29174563).
In vivo, is as efficient as vancomycin to protect mouse peritonitis models from MRSA infections (PubMed:29174563).

Features

Showing features for binding site.

194102030405060708090MKFSNISIAALFTILASTAMAAPAADSPDSIVAREPAPVEETYEAPSGLEKRGFGCPGSEKKCHNHCKSVKGYKGGYCDGPYIPFVGRPRCKCY
TypeIDPosition(s)Description
Binding site54beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate (UniProtKB | ChEBI)
Binding site55beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate (UniProtKB | ChEBI)
Binding site56beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate (UniProtKB | ChEBI)
Binding site66beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate (UniProtKB | ChEBI)
Binding site91beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componentmembrane
Cellular Componentother organism cell membrane
Molecular Functionlipid binding
Biological Processdefense response to bacterium

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Fungal defensin scedosporisin-2
  • Short names
    fDEF

Gene names

    • ORF names
      SAPIO_CDS6842

Organism names

Accessions

  • Primary accession
    A0A084G2W8

Proteomes

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis81-86Complete loss of antibacterial activity.

PTM/Processing

Features

Showing features for signal, propeptide, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-25
PropeptidePRO_000044942726-56
ChainPRO_000044942853-94Fungal defensin scedosporisin-2
Disulfide bond56↔78
Disulfide bond63↔91
Disulfide bond67↔93

Keywords

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region57-60Interaction site with membrane interface
Region83-90Interaction site with membrane interface

Domain

Has the structural arrangement of an alpha-helix connected to a beta-sheet by disulfide bonds (CSalpha/beta).

Sequence similarities

Belongs to the invertebrate defensin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    94
  • Mass (Da)
    10,048
  • Last updated
    2020-04-22 v2
  • Checksum
    FD8724AF2FB200DE
MKFSNISIAALFTILASTAMAAPAADSPDSIVAREPAPVEETYEAPSGLEKRGFGCPGSEKKCHNHCKSVKGYKGGYCDGPYIPFVGRPRCKCY

Sequence caution

The sequence KEZ41680.1 differs from that shown. Reason: Frameshift

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JOWA01000108
EMBL· GenBank· DDBJ
KEZ41680.1
EMBL· GenBank· DDBJ
Genomic DNA Frameshift

Genome annotation databases

Similar Proteins

Disclaimer

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