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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
Bacteria
Template P76343 (MSRQ_ECOLI)
Triggered by

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
msrQ

Comments [?]

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 FMN
Note: Binds 1 FMN per subunit.
heme b
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 [?]

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 [?]

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;

Computed features [?]

General Transmembrane; -; 6; trigger=yes;

Additional information [?]

Size range 197-220 amino acids
Related rules None
Fusion 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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