AC   MF_01207;
DC   Protein; auto
TR   HAMAP; MF_01207; -; 1; level=0
XX
Names: MsrQ
XX
ID   MSRQ
DE   RecName: Full=Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ;
DE   AltName: Full=Flavocytochrome MsrQ;
GN   Name=msrQ;
XX
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
CC   -!- FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic
CC       proteins containing methionine sulfoxide residues (Met-O), using
CC       respiratory chain electrons. Thus protects these proteins from
CC       oxidative-stress damage caused by reactive species of oxygen and
CC       chlorine generated by the host defense mechanisms. MsrPQ is essential
CC       for the maintenance of envelope integrity under bleach stress, rescuing
CC       a wide series of structurally unrelated periplasmic proteins from
CC       methionine oxidation, including the primary periplasmic chaperone SurA
CC       and the lipoprotein Pal. MsrQ provides electrons for reduction to the
CC       reductase catalytic subunit MsrP, using the quinone pool of the
CC       respiratory chain.
else case <OC:Pseudomonadota>
CC   -!- FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic
CC       proteins containing methionine sulfoxide residues (Met-O), using
CC       respiratory chain electrons. Thus protects these proteins from
CC       oxidative-stress damage caused by reactive species of oxygen and
CC       chlorine generated by the host defense mechanisms. MsrPQ is essential
CC       for the maintenance of envelope integrity under bleach stress, rescuing
CC       a wide series of structurally unrelated periplasmic proteins from
CC       methionine oxidation. MsrQ provides electrons for reduction to the
CC       reductase catalytic subunit MsrP, using the quinone pool of the
CC       respiratory chain.
else
CC   -!- FUNCTION: Part of the MsrPQ system that repairs oxidized cell envelope
CC       proteins containing methionine sulfoxide residues (Met-O), using
CC       respiratory chain electrons. Thus protects these proteins from
CC       oxidative-stress damage caused by reactive species of oxygen and
CC       chlorine. MsrPQ is essential for the maintenance of envelope integrity
CC       under bleach stress, rescuing a wide series of structurally unrelated
CC       cell envelope proteins from methionine oxidation. MsrQ provides
CC       electrons for reduction to the reductase catalytic subunit MsrP, using
CC       the quinone pool of the respiratory chain.
end case
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC       Note=Binds 1 FMN per subunit.;
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.;
CC   -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-binding
CC       subunit (MsrQ).
case not defined <Property:Membrane> or <Property:Membrane=1>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
else case <Property:Membrane=2>
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
end case
CC   -!- SIMILARITY: Belongs to the MsrQ family.
XX
DR   Pfam; PF01794; Ferric_reduct; 1; trigger=no
DR   General; Transmembrane; -; 6; trigger=yes
XX
case defined <Property:Membrane> and <Property:Membrane=2>
KW   Cell inner membrane
end case
KW   Cell membrane
KW   Electron transport
KW   Flavoprotein
KW   FMN
KW   Heme
KW   Iron
KW   Membrane
KW   Metal-binding
KW   Transmembrane
KW   Transport
KW   Transmembrane helix
XX
GO   GO:0009055; F:electron transfer activity
GO   GO:0010181; F:FMN binding
GO   GO:0020037; F:heme binding
GO   GO:0030091; P:protein repair
GO   GO:0005886; C:plasma membrane
XX
FT   None
XX
Size: 197-220;
Related: None;
Template: P76343;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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.
XX
# Revision 1.44 2023/01/26
//