ID   MSRQ_BRUA4              Reviewed;         220 AA.
AC   A6WYN0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=Oant_1367;
OS   Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS   LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC   15819 / NCTC 12168 / Alc 37;
RX   PubMed=21685287; DOI=10.1128/jb.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA   Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT   pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(2011).
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. {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; CP000758; ABS14084.1; -; Genomic_DNA.
DR   RefSeq; WP_010659435.1; NC_009667.1.
DR   AlphaFoldDB; A6WYN0; -.
DR   SMR; A6WYN0; -.
DR   STRING; 439375.Oant_1367; -.
DR   EnsemblBacteria; ABS14084; ABS14084; Oant_1367.
DR   GeneID; 61318129; -.
DR   KEGG; oan:Oant_1367; -.
DR   eggNOG; COG2717; Bacteria.
DR   HOGENOM; CLU_080662_2_0_5; -.
DR   OMA; LHFFWMR; -.
DR   OrthoDB; 1508607at2; -.
DR   PhylomeDB; A6WYN0; -.
DR   Proteomes; UP000002301; Chromosome 1.
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..220
FT                   /note="Protein-methionine-sulfoxide reductase heme-binding
FT                   subunit MsrQ"
FT                   /id="PRO_1000066178"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
SQ   SEQUENCE   220 AA;  24674 MW;  D51555A0BCF33715 CRC64;
     MAAAAQTGKK KTVRPGEWKI WLLYAVGFVP AVWTFYLGAS GNLGADPVKT FEHTLGLWAL
     RFLILTLMVT PIRDLTGMAF LRYRRALGLL AFYYALMHFA TYMVLDQGLN ISAIVTDIVR
     RPFITIGMIS LVLLVPLALT SNNWSIRKLG RRWNSLHKLV YVAIAGGAIH FIMSVKSWPA
     EPVIYAGIVS ALLLWRLVRP HARNRKPVSR PRGEAMAVKK