ID A0A3D8VFV1_9GAMM Unreviewed; 214 AA.
AC A0A3D8VFV1;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=DX912_06205 {ECO:0000313|EMBL:RDY68195.1};
OS Lysobacter soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=453783 {ECO:0000313|EMBL:RDY68195.1, ECO:0000313|Proteomes:UP000256829};
RN [1] {ECO:0000313|EMBL:RDY68195.1, ECO:0000313|Proteomes:UP000256829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22011 {ECO:0000313|EMBL:RDY68195.1,
RC ECO:0000313|Proteomes:UP000256829};
RA Zhang X., Feng G., Zhu H.;
RT "Lysobacter soli KCTC 22011, whole genome shotgun sequence.";
RL Submitted (AUG-2018) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01207}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDY68195.1}.
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DR EMBL; QTJR01000003; RDY68195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8VFV1; -.
DR Proteomes; UP000256829; 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:UP000256829};
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 56..74
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 86..104
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 124..145
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 157..175
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 181..200
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT DOMAIN 53..167
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
SQ SEQUENCE 214 AA; 24124 MW; A27B3DE9ABADBA3A CRC64;
MPLSSRTLIA IKTLVHALAL TPAAILAWQI RAEFLTGSGG LGADPVAEIE HRLGLWALRF
LMLTLAITPL RQLTGQPVLL RFRRMLGLYA FAYATLHFTA YLVLDLRGYW TQIFEEIAKR
PYITVGFAAW LLLVPLALTS TQAAIRWLGR NWARLHKLVY VIAMLAVLHF WWLVKSDVRE
PALYAGILAV LLGWRAWNAL KKRKLSARRK AAAG
//
