B7USY1 · MSRP_ECO27
- ProteinProtein-methionine-sulfoxide reductase catalytic subunit MsrP
- GenemsrP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids334 (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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. 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-(S)-S-oxide-[protein] + a quinol
- L-methionyl-[protein] + a quinone + H2O = L-methionyl-(R)-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 | 88 | Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 91-92 | Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 146 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 181 | Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 233 | Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 238 | Mo-molybdopterin (UniProtKB | ChEBI) | |||
Binding site | 249-251 | Mo-molybdopterin (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | periplasmic space | |
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionB7USY1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Is attached to the inner membrane when interacting with the MsrQ subunit.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-44 | Tat-type signal | |||
Chain | PRO_1000164656 | 45-334 | Protein-methionine-sulfoxide reductase catalytic subunit MsrP | ||
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
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length334
- Mass (Da)37,314
- Last updated2009-02-10 v1
- MD5 Checksum19697E8A448F23D0CC03712B5A17DE6C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FM180568 EMBL· GenBank· DDBJ | CAS09630.1 EMBL· GenBank· DDBJ | Genomic DNA |