HAMAP rule MF_01207
General rule information
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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
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Identifier, protein and gene names
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Identifier | MSRQ |
Protein name | RecName: Full=Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; AltName: Full=Flavocytochrome MsrQ; |
Gene name | Name=msrQ; |
Comments
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case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella> | |
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. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain. |
else case <OC:Pseudomonadota> | |
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. |
else | |
FUNCTION | Part 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.; |
SUBUNIT | Heterodimer of a catalytic subunit (MsrP) and a heme-binding subunit (MsrQ). |
case not defined <Property:Membrane> or <Property:Membrane=1> | |
SUBCELLULAR LOCATION | Cell membrane; Multi-pass membrane protein. |
else case <Property:Membrane=2> | |
SUBCELLULAR LOCATION | Cell inner membrane; Multi-pass membrane protein. |
end case | |
SIMILARITY | Belongs to the MsrQ family. |
Keywords
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case defined <Property:Membrane> and <Property:Membrane=2> | |
Cell inner membrane | |
end case | |
Cell membrane | |
Electron transport | |
Flavoprotein | |
FMN | |
Heme | |
Iron | |
Membrane | |
Metal-binding | |
Transmembrane | |
Transport | |
Transmembrane helix |
Gene Ontology
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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
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Pfam | PF01794; Ferric_reduct; 1; |
General | Transmembrane; -; 6; |
Features
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Additional information
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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. |