(data stored in SCRATCH9089 zone)

SWISSPROT: MSRQ_PASMU

ID   MSRQ_PASMU              Reviewed;         206 AA.
AC   Q9CN97;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 105.
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=PM0538;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
DR   EMBL; AE004439; AAK02622.1; -; Genomic_DNA.
DR   RefSeq; WP_010906713.1; NC_002663.1.
DR   EnsemblBacteria; AAK02622; AAK02622; PM0538.
DR   KEGG; pmu:PM0538; -.
DR   PATRIC; fig|272843.6.peg.545; -.
DR   eggNOG; ENOG4105DQ2; Bacteria.
DR   eggNOG; COG2717; LUCA.
DR   HOGENOM; HOG000255015; -.
DR   KO; K17247; -.
DR   OMA; LHFFWMR; -.
DR   BioCyc; PMUL272843:G1FZ8-569-MONOMER; -.
DR   Proteomes; UP000000809; 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;
DR   PRODOM; Q9CN97.
DR   SWISS-2DPAGE; Q9CN97.
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..206
FT                   /note="Protein-methionine-sulfoxide reductase heme-binding
FT                   subunit MsrQ"
FT                   /id="PRO_0000091577"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
SQ   SEQUENCE   206 AA;  23653 MW;  2F277729D7F11194 CRC64;
     MLSLFRIIIH VCCLGPVAWL AWVLLSGDES QLGADPIKEI QHFLGFSALT ILLIMFILGK
     VFYLLKQPQL QVLRRALGLW AWFYVVLHVY AYLALELGYD FSLFVQELVN RGYLIIGAIA
     FLILTLMALS SWSYLKLKMG KWWFYLHQLG YYALLLGAIH YVWSVKNVTF SSMLYLILSI
     MILCDALYGL FIKRKGRSTS AHTGKD
//

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