ID A0A3S0PL09_9BURK Unreviewed; 209 AA.
AC A0A3S0PL09;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 03-MAY-2023, entry version 11.
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=EKL30_12340 {ECO:0000313|EMBL:RTZ42487.1};
OS Candidimonas sp. SYP-B2681.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Candidimonas.
OX NCBI_TaxID=2497686 {ECO:0000313|EMBL:RTZ42487.1, ECO:0000313|Proteomes:UP000288599};
RN [1] {ECO:0000313|EMBL:RTZ42487.1, ECO:0000313|Proteomes:UP000288599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SYP-B2681 {ECO:0000313|EMBL:RTZ42487.1,
RC ECO:0000313|Proteomes:UP000288599};
RA Zhang M.-Y., Zhang Y.-X.;
RT "Candidimonas lamiisoli sp. nov., a novel bacterium can accelerate seed
RT germination.";
RL Submitted (DEC-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: 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:RTZ42487.1}.
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DR EMBL; RYDV01000005; RTZ42487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0PL09; -.
DR OrthoDB; 9788328at2; -.
DR Proteomes; UP000288599; 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:UP000288599};
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 21..37
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 57..76
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 88..106
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 126..145
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 157..174
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 186..204
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT DOMAIN 56..168
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
SQ SEQUENCE 209 AA; 24373 MW; F36C64D424BC7B22 CRC64;
MPASTPGRVN WTSKNVAQIK PLVFILALYP VFRWVWLGFT DGLSANPAEF LIRSSGIWAL
VALLLTLTIT PLRRIFQQPA LVRLRRMLGL FAFFYTCLHL LGWAFWERDW SLASMWDDIV
QRTFILIGMI AFVPMVALAC TSTRGWMHRM GHHWQSLHRS IYLIAALSVW HFWLVRAGKN
DFFDPYVYGV VLAVLLLVRV WFFVRRRTS
//
