A0A084G2W8 · DEFS2_PSEDA
- ProteinFungal defensin scedosporisin-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score3/5
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).
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 54 | beta-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 site | 55 | beta-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 site | 56 | beta-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 site | 66 | beta-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 site | 91 | beta-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
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Cellular Component | other organism cell membrane | |
Molecular Function | lipid binding | |
Biological Process | defense response to bacterium |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameFungal defensin scedosporisin-2
- Short namesfDEF
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Microascales > Microascaceae > Scedosporium
Accessions
- Primary accessionA0A084G2W8
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 81-86 | Complete loss of antibacterial activity. | |||
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-25 | ||||
Propeptide | PRO_0000449427 | 26-56 | |||
Chain | PRO_0000449428 | 53-94 | Fungal defensin scedosporisin-2 | ||
Disulfide bond | 56↔78 | ||||
Disulfide bond | 63↔91 | ||||
Disulfide bond | 67↔93 | ||||
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 57-60 | Interaction site with membrane interface | |||
Region | 83-90 | Interaction 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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length94
- Mass (Da)10,048
- Last updated2020-04-22 v2
- ChecksumFD8724AF2FB200DE
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JOWA01000108 EMBL· GenBank· DDBJ | KEZ41680.1 EMBL· GenBank· DDBJ | Genomic DNA | Frameshift |