A0A926NU52 · A0A926NU52_9HYPH
- ProteinProtein-methionine-sulfoxide reductase heme-binding subunit MsrQ
- GenemsrQ
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids293 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FMN per subunit.
Note: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | electron transfer activity | |
Molecular Function | FMN binding | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on diphenols and related substances as donors | |
Biological Process | protein repair |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameProtein-methionine-sulfoxide reductase heme-binding subunit MsrQ
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Stappiaceae > Roseibium
Accessions
- Primary accessionA0A926NU52
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 28-50 | Helical | ||||
Sequence: LAVFIGLLVPAVAIFADLIFGPM | ||||||
Transmembrane | 65-83 | Helical | ||||
Sequence: WVVRFLLLSLAITPFRRIL | ||||||
Transmembrane | 95-113 | Helical | ||||
Sequence: IGVSVLCYALLHLGFYAAQ | ||||||
Transmembrane | 125-150 | Helical | ||||
Sequence: IVLRVYLTIGFAALLGLIALGATSFD | ||||||
Transmembrane | 162-180 | Helical | ||||
Sequence: LLHRLAYVIGVLALIHFFM | ||||||
Transmembrane | 186-205 | Helical | ||||
Sequence: VTEPTLMAGLFILLMSYRVA | ||||||
Transmembrane | 217-239 | Helical | ||||
Sequence: VLGLCAAISAALTAGVEYSWYAI | ||||||
Transmembrane | 259-282 | Helical | ||||
Sequence: IRPAVWVAIIGIAVASLPLLRMLL |
Keywords
- Cellular component
Interaction
Subunit
Heterodimer of a catalytic subunit (MsrP) and a heme-binding subunit (MsrQ).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 63-174 | Ferric oxidoreductase | ||||
Sequence: GRWVVRFLLLSLAITPFRRILGWNRLIGVRRMIGVSVLCYALLHLGFYAAQENWHLGKVASEIVLRVYLTIGFAALLGLIALGATSFDAAVRRMGRNWNLLHRLAYVIGVLA |
Sequence similarities
Belongs to the MsrQ family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length293
- Mass (Da)32,128
- Last updated2023-02-22 v1
- ChecksumBB2F11020A04F932