ID   MSRQ_AZOOP              Reviewed;         233 AA.
AC   G8QMC1;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   03-AUG-2022, entry version 52.
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};
GN   Synonyms=yedZ2 {ECO:0000303|PubMed:25968643}; OrderedLocusNames=Dsui_1299;
OS   Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS) (Dechlorosoma
OS   suillum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Azospira.
OX   NCBI_TaxID=640081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-33 / DSM 13638 / PS;
RX   PubMed=22535943; DOI=10.1128/jb.00124-12;
RA   Byrne-Bailey K.G., Coates J.D.;
RT   "Complete genome sequence of the anaerobic perchlorate-reducing bacterium
RT   Azospira suillum strain PS.";
RL   J. Bacteriol. 194:2767-2768(2012).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC BAA-33 / DSM 13638 / PS;
RX   PubMed=25968643; DOI=10.1128/mbio.00233-15;
RA   Melnyk R.A., Youngblut M.D., Clark I.C., Carlson H.K., Wetmore K.M.,
RA   Price M.N., Iavarone A.T., Deutschbauer A.M., Arkin A.P., Coates J.D.;
RT   "Novel mechanism for scavenging of hypochlorite involving a periplasmic
RT   methionine-rich peptide and methionine sulfoxide reductase.";
RL   MBio 6:E00233-E00233(2015).
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 (By similarity). Probably involved in protection
CC       against reactive chlorine species (RCS) generated by chlorite and
CC       hypochlorite (PubMed:25968643). {ECO:0000255|HAMAP-Rule:MF_01207,
CC       ECO:0000305|PubMed:25968643}.
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; CP003153; AEV25699.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8QMC1; -.
DR   STRING; 640081.Dsui_1299; -.
DR   EnsemblBacteria; AEV25699; AEV25699; Dsui_1299.
DR   KEGG; dsu:Dsui_1299; -.
DR   eggNOG; COG2717; Bacteria.
DR   HOGENOM; CLU_080662_0_1_4; -.
DR   OMA; LHFFWMR; -.
DR   Proteomes; UP000005633; 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..233
FT                   /note="Protein-methionine-sulfoxide reductase heme-binding
FT                   subunit MsrQ"
FT                   /id="PRO_0000440892"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          50..164
FT                   /note="Ferric oxidoreductase"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   233 AA;  26320 MW;  4E0E6D70B2A2A156 CRC64;
     MTFQPTPRQL SAIKAALFLL TLLPALHYAH GLWSDSLGAN PIEALTRGMG IWTLNFLFLT
     LCVSPLRKLS GWHWLLRLRR MLGLTAFAYG CLHLLTYLWL DQFWDVDAIA RDIWKRPFIT
     VGATAFLLML PLALTSSHAA IRSLGGKRWQ SLHRAVYAVA ILGVVHYLWL VKRVALLDPI
     IYALVLAILL GWRVVERIRL NGPWPTRSTP PAVQPVVFMK RDAVAALGEP KKR