ID F4GXJ4_PUSST Unreviewed; 212 AA.
AC F4GXJ4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ {ECO:0000256|HAMAP-Rule:MF_01207};
DE AltName: Full=Flavocytochrome MsrQ {ECO:0000256|HAMAP-Rule:MF_01207};
GN Name=msrQ {ECO:0000256|HAMAP-Rule:MF_01207};
GN OrderedLocusNames=PT7_1702 {ECO:0000313|EMBL:AEC20242.1};
OS Pusillimonas sp. (strain T7-7).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pusillimonas.
OX NCBI_TaxID=1007105 {ECO:0000313|EMBL:AEC20242.1, ECO:0000313|Proteomes:UP000008737};
RN [1] {ECO:0000313|EMBL:AEC20242.1, ECO:0000313|Proteomes:UP000008737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T7-7 {ECO:0000313|EMBL:AEC20242.1,
RC ECO:0000313|Proteomes:UP000008737};
RX PubMed=21622753; DOI=10.1128/JB.05242-11;
RA Cao B., Ma T., Ren Y., Ren Y., Li G., Li P., Guo X., Ding P., Feng L.;
RT "Complete genome sequence of Pusillimonas sp. T7-7, a cold-tolerant diesel
RT oil-degrading bacterium isolated from the Bohai Sea in China.";
RL J. Bacteriol. 193:4021-4022(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T7-7;
RA Cao B., Ma T., Li P., Jiang L., Li Y., Guo X., Feng L.;
RT "Genome Announcement Complete Genome Sequence of Pusillimonas sp. T7-7, a
RT novel species isolated from the Bohai Sea, China.";
RL Submitted (APR-2011) 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:0000256|HAMAP-Rule:MF_01207}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01207};
CC Note=Binds 1 FMN per subunit. {ECO:0000256|HAMAP-Rule:MF_01207};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01207};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000256|HAMAP-Rule:MF_01207};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-binding
CC subunit (MsrQ). {ECO:0000256|HAMAP-Rule:MF_01207}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01207}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01207}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the MsrQ family. {ECO:0000256|HAMAP-
CC Rule:MF_01207}.
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DR EMBL; CP002663; AEC20242.1; -; Genomic_DNA.
DR RefSeq; WP_013742778.1; NC_015458.1.
DR AlphaFoldDB; F4GXJ4; -.
DR STRING; 1007105.PT7_1702; -.
DR KEGG; put:PT7_1702; -.
DR eggNOG; COG2717; Bacteria.
DR HOGENOM; CLU_080662_0_0_4; -.
DR OrthoDB; 9788328at2; -.
DR Proteomes; UP000008737; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; PROTEIN-METHIONINE-SULFOXIDE REDUCTASE HEME-BINDING SUBUNIT MSRQ; 1.
DR PANTHER; PTHR36964:SF1; PROTEIN-METHIONINE-SULFOXIDE REDUCTASE HEME-BINDING SUBUNIT MSRQ; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01207};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01207};
KW Electron transport {ECO:0000256|HAMAP-Rule:MF_01207};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01207};
KW FMN {ECO:0000256|HAMAP-Rule:MF_01207};
KW Heme {ECO:0000256|HAMAP-Rule:MF_01207};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01207};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01207};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01207};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01207};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01207};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01207}.
FT TRANSMEM 22..39
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 91..109
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 129..150
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 162..177
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 189..207
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT DOMAIN 58..171
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
SQ SEQUENCE 212 AA; 24486 MW; D576BE0C61E8AD88 CRC64;
MSAQEAVVPG ARNWTAQEVA RIKPLVFLLA LYPLVRWIWL GTHDGLSANP PEFLIRSSGI
WALVLLGLTL CVTPLRRLIS QPALVRLRRM LGLFAFFYTC LHVLGWAYWE RGWSLVSMWD
DIVQRTFILV GMIAFVPMAA LAMTSTRGWI HRLGRGWQQL HRSVYLIAIL SVWHFWLVRA
GKNDFSEPYL YGAMLAVLLL IRIIFFYRRR SA
//
