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HAMAP rule MF_01207

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General rule information [?]

Accession MF_01207
Dates 18-MAR-2002 (Created)
26-JAN-2023 (Last updated, Version 44)
Name MsrQ
Scope(s) Bacteria
Template(s) P76343 (MSRQ_ECOLI); [ Recover all ]
Triggered by HAMAP; MF_01207 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier MSRQ
Protein name RecName: Full=Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ;
AltName: Full=Flavocytochrome MsrQ;
Gene name Name=msrQ;

Comments [?]

case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
FUNCTIONPart 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. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
else case <OC:Pseudomonadota>
FUNCTIONPart 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.
else
FUNCTIONPart of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
end case
COFACTOR Name=FMN; Xref=ChEBI:CHEBI:58210; Note=Binds 1 FMN per subunit.;
COFACTOR Name=heme b; Xref=ChEBI:CHEBI:60344; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
SUBUNITHeterodimer of a catalytic subunit (MsrP) and a heme-binding subunit (MsrQ).
case not defined <Property:Membrane> or <Property:Membrane=1>
SUBCELLULAR LOCATIONCell membrane; Multi-pass membrane protein.
else case <Property:Membrane=2>
SUBCELLULAR LOCATIONCell inner membrane; Multi-pass membrane protein.
end case
SIMILARITYBelongs to the MsrQ family.

Keywords [?]


Gene Ontology [?]

GO:0009055; Molecular function:electron transfer activity
GO:0010181; Molecular function:FMN binding
GO:0020037; Molecular function:heme binding
GO:0030091; Biological process:protein repair
GO:0005886; Cellular component:plasma membrane

Cross-references [?]

Pfam PF01794; Ferric_reduct; 1;
General Transmembrane; -; 6;

Features [?]


Additional information [?]

Size range 197-220 amino acids
Related rules None
Fusion Nter: None Cter: None
Comments The C-terminus of MamZ, a protein involved in magnetosome formation in magnetotactic bacteria, matches this rule. It is about 3 times longer however and should not by annotated by this rule.



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