ID   MSRQ_SALAR              Reviewed;         199 AA.
AC   A9MNV6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ {ECO:0000255|HAMAP-Rule:MF_01207};
DE   AltName: Full=Flavocytochrome MsrQ {ECO:0000255|HAMAP-Rule:MF_01207};
GN   Name=msrQ {ECO:0000255|HAMAP-Rule:MF_01207}; OrderedLocusNames=SARI_04255;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_01207}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01207};
CC       Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01207};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01207};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01207};
CC   -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-binding
CC       subunit (MsrQ). {ECO:0000255|HAMAP-Rule:MF_01207}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01207}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01207}.
CC   -!- SIMILARITY: Belongs to the MsrQ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01207}.
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DR   EMBL; CP000880; ABX24038.1; -; Genomic_DNA.
DR   RefSeq; WP_001240049.1; NC_010067.1.
DR   AlphaFoldDB; A9MNV6; -.
DR   STRING; 41514.SARI_04255; -.
DR   EnsemblBacteria; ABX24038; ABX24038; SARI_04255.
DR   KEGG; ses:SARI_04255; -.
DR   HOGENOM; CLU_080662_1_0_6; -.
DR   OMA; LHFFWMR; -.
DR   OrthoDB; 1508607at2; -.
DR   Proteomes; UP000002084; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01207; MsrQ; 1.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR022837; MsrQ-like.
DR   PANTHER; PTHR36964; PTHR36964; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Electron transport; Flavoprotein; FMN;
KW   Heme; Iron; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..199
FT                   /note="Protein-methionine-sulfoxide reductase heme-binding
FT                   subunit MsrQ"
FT                   /id="PRO_1000085531"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
SQ   SEQUENCE   199 AA;  22855 MW;  71CE13FF70EFE95B CRC64;
     MRLTAKQIIW LKVCLHLVGF LPLLWLFWAI NQGGLSADPV KDIQHFTGRT ALKFLLATLL
     ISPLARYAKQ PLLIRTRRLL GLWCFVWATL HLTSYALLEL GIHNLALLGS ELISRPYLTL
     GIISWLALLA LTLTSTQFAQ RKLGKRWQTL HNVVYLVAIL APVHYLWSVK VLSPQPVIYA
     ALALVLLALR YRKFRQWRR