ID   MSRQ_SERP5              Reviewed;         199 AA.
AC   A8GK69;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=Spro_4415;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-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. 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; CP000826; ABV43509.1; -; Genomic_DNA.
DR   RefSeq; WP_012147110.1; NC_009832.1.
DR   AlphaFoldDB; A8GK69; -.
DR   SMR; A8GK69; -.
DR   STRING; 399741.Spro_4415; -.
DR   EnsemblBacteria; ABV43509; ABV43509; Spro_4415.
DR   KEGG; spe:Spro_4415; -.
DR   eggNOG; COG2717; Bacteria.
DR   HOGENOM; CLU_080662_1_0_6; -.
DR   OMA; LHFFWMR; -.
DR   OrthoDB; 1508607at2; -.
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..199
FT                   /note="Protein-methionine-sulfoxide reductase heme-binding
FT                   subunit MsrQ"
FT                   /id="PRO_1000066186"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
SQ   SEQUENCE   199 AA;  22873 MW;  08720B018C64885E CRC64;
     MRLTPTHIKG IKVAIYLAAF LPFLWLVLSV DQGWFSADPA KDIQHFTGRM TLKLLLATLM
     IAPLARYTRQ PLLIRCRRLV GLWCFAWGTL HLISYSTLEL GLSNIGLLGR ELVTRPYLTL
     GIISWLILLA LAATSTLWAM RKLGAKWQTL HNLVYLVAIL APIHYLWSVK TFSPQPFIYA
     LLAVVLLALR YKKFRNWWR