MSRQ_BRUSU
ID MSRQ_BRUSU Reviewed; 220 AA.
AC Q8FV59; G0KDZ8;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 96.
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 OrderedLocusNames=BRA0991, BS1330_II0983;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(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; AE014292; AAN34160.1; -; Genomic_DNA.
DR EMBL; CP002998; AEM20436.1; -; Genomic_DNA.
DR RefSeq; WP_002965660.1; NZ_KN046805.1.
DR AlphaFoldDB; Q8FV59; -.
DR EnsemblBacteria; AEM20436; AEM20436; BS1330_II0983.
DR GeneID; 45126294; -.
DR GeneID; 55592616; -.
DR KEGG; bms:BRA0991; -.
DR KEGG; bsi:BS1330_II0983; -.
DR PATRIC; fig|204722.21.peg.1133; -.
DR HOGENOM; CLU_080662_2_0_5; -.
DR OMA; LHFFWMR; -.
DR PhylomeDB; Q8FV59; -.
DR Proteomes; UP000007104; Chromosome II.
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; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..220
FT /note="Protein-methionine-sulfoxide reductase heme-binding
FT subunit MsrQ"
FT /id="PRO_0000091571"
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 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
SQ SEQUENCE 220 AA; 24797 MW; AC2C060433169497 CRC64;
MAAATGTRKK KTPRPGQWKL WLLYTAGFVP AVWTFYLGAT GQLGADPVKT FEHLLGLWAL
RFLILTLLVT PIRDLTGITL LRYRRALGLL AFYYALMHFT TYMVLDQGLN LSAIITDIVR
RPFITIGMIS LALLVPLALT SNNWSIRKLG RRWSSLHKLV YIAIAGSAVH FLMSVKSWPA
EPVIYAAIVA ALLLWRLARP YLRTRKPALR PRGEAIALRK
