B4SUN2 · MSRP_SALNS
- 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
- a quinone + H2O + L-methionyl-[protein] = a quinol + L-methionyl-(S)-S-oxide-[protein]
- a quinone + H2O + L-methionyl-[protein] = a quinol + L-methionyl-(R)-S-oxide-[protein]
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) | ||||
Sequence: N | ||||||
Binding site | 91-92 | Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: YE | ||||||
Binding site | 146 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 181 | Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 233 | Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 238 | Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 249-251 | Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: GIK |
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 > Salmonella
Accessions
- Primary accessionB4SUN2
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 | ||||
Sequence: MKKIRPLTEADVTAESAFFMQRRQVLKALGISAAALSLPSTAQA | ||||||
Chain | PRO_1000138723 | 45-334 | Protein-methionine-sulfoxide reductase catalytic subunit MsrP | |||
Sequence: DLFSWFKGNDRPKAPAGKPLEFSQPAAWRSDLALTPEDKVTGYNNFYEFGLDKADPAANAGSLKTEPWTLKISGEVAKPFTLDYDDLTHRFPLEERIYRMRCVEAWSMVVPWIGFPLYKLLAQAQPTSHAKYVAFETLYAPDDMPGQKDRFIGGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPIRLIVPWKYGFKGIKSIVSIKLTRERPPTTWNLSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILDVQRQPTLLFNGYANEVASLYRGLNLRENF |
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)37,492
- Last updated2008-09-23 v1
- ChecksumEDC459B96461A08C
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001113 EMBL· GenBank· DDBJ | ACF64022.1 EMBL· GenBank· DDBJ | Genomic DNA |