A0A1F4AZU7 · A0A1F4AZU7_9PROT
- ProteinProtein-methionine-sulfoxide reductase catalytic subunit MsrP
- GenemsrP
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids315 (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. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide.
Catalytic activity
- L-methionyl-[protein] + a quinone + H2O = L-methionyl-(R)-S-oxide-[protein] + a quinol
- L-methionyl-[protein] + a quinone + H2O = L-methionyl-(S)-S-oxide-[protein] + a quinol
Cofactor
Note: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 78 | Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 81-82 | Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 135 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 170 | Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 218 | Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 223 | Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 234-236 | Mo-molybdopterin (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | molybdopterin cofactor binding | |
Molecular Function | oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor | |
Biological Process | protein repair |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein-methionine-sulfoxide reductase catalytic subunit MsrP
- EC number
Gene names
Organism names
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria
Accessions
- Primary accessionA0A1F4AZU7
Proteomes
PTM/Processing
Post-translational modification
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Interaction
Subunit
Heterodimer of a catalytic subunit (MsrP) and a heme-binding subunit (MsrQ).
Structure
Sequence
- Sequence statusComplete
- Length315
- Mass (Da)36,242
- Last updated2017-02-15 v1
- MD5 Checksum13F0E7E59DB9DBEB335DE5515F373D1C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MERA01000360 EMBL· GenBank· DDBJ | OGA17539.1 EMBL· GenBank· DDBJ | Genomic DNA |