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Database: UniProt
Entry: A0A1I1UEY2_9GAMM
LinkDB: A0A1I1UEY2_9GAMM
Original site: A0A1I1UEY2_9GAMM 
ID   A0A1I1UEY2_9GAMM        Unreviewed;       202 AA.
AC   A0A1I1UEY2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
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   ORFNames=SAMN05660831_02050 {ECO:0000313|EMBL:SFD66510.1};
OS   Thiohalospira halophila DSM 15071.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thiohalospira.
OX   NCBI_TaxID=1123397 {ECO:0000313|EMBL:SFD66510.1, ECO:0000313|Proteomes:UP000198611};
RN   [1] {ECO:0000313|EMBL:SFD66510.1, ECO:0000313|Proteomes:UP000198611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL3 {ECO:0000313|EMBL:SFD66510.1,
RC   ECO:0000313|Proteomes:UP000198611};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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 membrane {ECO:0000256|HAMAP-Rule:MF_01207};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01207}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the MsrQ family. {ECO:0000256|HAMAP-
CC       Rule:MF_01207}.
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DR   EMBL; FOMJ01000007; SFD66510.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1UEY2; -.
DR   STRING; 1123397.SAMN05660831_02050; -.
DR   OrthoDB; 9788328at2; -.
DR   Proteomes; UP000198611; Unassembled WGS sequence.
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 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|ARBA:ARBA00022617, 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   Reference proteome {ECO:0000313|Proteomes:UP000198611};
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        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT   TRANSMEM        49..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT   TRANSMEM        78..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT   TRANSMEM        113..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT   TRANSMEM        152..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT   DOMAIN          47..160
FT                   /note="Ferric oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01794"
SQ   SEQUENCE   202 AA;  23206 MW;  B9CD0BAD697F6629 CRC64;
     MRRQTVRYRL KPAVFGLASL PALWLVWGAF TGGLGTNPAE TLIVESGTWT LRMLLIGLAL
     TPLRGLTGWN WPMQLRRMLG LFAFFYAAAH LTLYLWLDQF FWWTEIARDI LERPFITVGL
     LAFTLLLPLA LTSPRAAVKR LGAKRWQALH RLVYPAAVAG VVHHWWIVRA DYREAMVHAI
     IMTLLLGYRL VFGWAPRILQ RN
//
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