UniProtKB - P82042 (UPE35_UPEMJ)
Uperin-3.5
Functioni
Shows antibacterial activity against B.cereus, L.lactis, L.innocua, M.luteus, S.aureus, P.multoci, S.hominis, S.epidermidis and S.uberis (Ref. 1, PubMed:33431675). Strong activity against M.luteus (MIC=2 µM) compared to S.hominis, S.epidermidis and S.aureus (PubMed:33431675).
Acts by inducing permeabilization of bacterial membranes (PubMed:33431675).
Forms amyloid fibrils which, in the presence of bacteria, aggregate on the bacterial membrane leading to severe membrane damage and cell death (Ref. 3, PubMed:33431675).
3 PublicationsMiscellaneous
Temperature dependencei
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 7 | Involved in inter-helical interactions along the fibril1 Publication | 1 |
GO - Molecular functioni
- protein homodimerization activity Source: UniProtKB
GO - Biological processi
- cytolysis in another organism Source: UniProtKB
- defense response to Gram-positive bacterium Source: UniProtKB
- membrane disruption in another organism Source: UniProtKB
Keywordsi
Molecular function | Amphibian defense peptide, Antibiotic, Antimicrobial |
Names & Taxonomyi
Protein namesi | Recommended name: Uperin-3.51 Publication |
Organismi | Uperoleia mjobergii (Mjoberg's toadlet) (Pseudophryne mjobergii) |
Taxonomic identifieri | 104954 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Myobatrachoidea › Myobatrachidae › Myobatrachinae › Uperoleia |
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Other locations
- Target cell membrane 2 Publications
Note: Secreted monomers and fibrils appear to be able to interact with target cell membranes.2 Publications
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Other locations
- membrane Source: UniProtKB-KW
- other organism cell membrane Source: UniProtKB
Keywords - Cellular componenti
Membrane, Secreted, Target cell membrane, Target membranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 1 | G → L: Loss of amyloid fibril formation but no effect on membrane disruption activity against bacterial mimetic membranes (DMPC:DMPG). Displays a significant increase in amyloid fibril formation; when associated with A-7. 2 Publications | 1 | |
Mutagenesisi | 4 | D → A: Decreased amyloid fibril formation. 1 Publication | 1 | |
Mutagenesisi | 7 | R → A: Loss of membrane disruption activity against bacterial mimetic membranes (DMPC:DMPG) and strong increase in amyloid fibril formation. Displays a significant increase in amyloid fibril formation; when associated with L-1. 2 Publications | 1 | |
Mutagenesisi | 7 | R → K: No effect on membrane disruption activity against bacterial mimetic membranes (DMPC:DMPG) or amyloid fibril formation. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
PeptideiPRO_0000043858 | 1 – 17 | Uperin-3.5Add BLAST | 17 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 17 | Valine amide1 Publication | 1 |
Keywords - PTMi
AmidationExpressioni
Tissue specificityi
Interactioni
Subunit structurei
Monomer and homodimer (PubMed:26676975, PubMed:33431675). Assembles into amyloid fibrils (PubMed:26676975, Ref. 3, PubMed:31385514, PubMed:33431675). Under lipid-free conditions, mostly forms fibrils with a cross-beta architecture, consisting of stacks of monomeric amphipathic beta-helices arranged in an antiparallel manner (PubMed:26676975, PubMed:31385514, PubMed:33431675). In the presence of bacteria or membrane lipids, fibrils switch to a cross-alpha conformation which may correlate with its antibacterial activity (PubMed:26676975, Ref. 3, PubMed:31385514, PubMed:33431675).
4 PublicationsGO - Molecular functioni
- protein homodimerization activity Source: UniProtKB
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P82042 |
SMRi | P82042 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Family and domain databases
InterProi | View protein in InterPro IPR012527, Antimicrobial_8 |
Pfami | View protein in Pfam PF08103, Antimicrobial_8, 1 hit |
i Sequence
Sequence statusi: Complete.
Mass spectrometryi
Cross-referencesi
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6GS3 | X-ray | 1.45 | A/B | 1-17 | [»] | |
AlphaFoldDBi | P82042 | |||||
SMRi | P82042 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Family and domain databases
InterProi | View protein in InterPro IPR012527, Antimicrobial_8 |
Pfami | View protein in Pfam PF08103, Antimicrobial_8, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | UPE35_UPEMJ | |
Accessioni | P82042Primary (citable) accession number: P82042 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
Last sequence update: | May 30, 2000 | |
Last modified: | May 25, 2022 | |
This is version 47 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references