ID A0A1M6NHS8_9RHOB Unreviewed; 199 AA.
AC A0A1M6NHS8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN05444000_1163 {ECO:0000313|EMBL:SHJ95291.1};
OS Shimia gijangensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1470563 {ECO:0000313|EMBL:SHJ95291.1, ECO:0000313|Proteomes:UP000183982};
RN [1] {ECO:0000313|Proteomes:UP000183982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100564 {ECO:0000313|Proteomes:UP000183982};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; FQZQ01000016; SHJ95291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6NHS8; -.
DR STRING; 1470563.SAMN05444000_1163; -.
DR Proteomes; UP000183982; 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|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:UP000183982};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 50..68
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 80..99
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 119..137
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 149..167
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 173..190
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT DOMAIN 56..160
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
SQ SEQUENCE 199 AA; 22168 MW; 54BA9A7C1278F494 CRC64;
MIAYLNQAAK KLPTWPLYVV GALYPAWLLW QGLTGGLGVD PVKEMEHALG EAGLQLLIAG
LCITPLRRHA GVNLLRFRRA IGLLAFTYIC LHLLVWLVLD VQIASQILAD ILKRPYVTIG
MAGFVLLIPL AVTSNNLSIR RLGRTWHRLH KLTYAATLLG ALHFVMLVKG FQIEPLIYMG
VTVCVLALRI RPRAFRKVA
//
