ID J2M1N1_9BURK Unreviewed; 224 AA.
AC J2M1N1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=PMI16_01560 {ECO:0000313|EMBL:EJL91603.1};
OS Herbaspirillum sp. CF444.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1144319 {ECO:0000313|EMBL:EJL91603.1, ECO:0000313|Proteomes:UP000007296};
RN [1] {ECO:0000313|EMBL:EJL91603.1, ECO:0000313|Proteomes:UP000007296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF444 {ECO:0000313|EMBL:EJL91603.1,
RC ECO:0000313|Proteomes:UP000007296};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL91603.1}.
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DR EMBL; AKJW01000030; EJL91603.1; -; Genomic_DNA.
DR RefSeq; WP_007878155.1; NZ_AKJW01000030.1.
DR AlphaFoldDB; J2M1N1; -.
DR STRING; 1144319.PMI16_01560; -.
DR PATRIC; fig|1144319.3.peg.1586; -.
DR eggNOG; COG2717; Bacteria.
DR OrthoDB; 9788328at2; -.
DR Proteomes; UP000007296; 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 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..34
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 54..72
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 84..101
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 153..172
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01207"
FT DOMAIN 51..165
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
SQ SEQUENCE 224 AA; 26141 MW; 00AE88867B6D3C93 CRC64;
MNALKTLSTR QVLYLRNVLF VLALMPLARL VLFVFLDKLG ANPIEFITRN TGDWALYFLT
ITLAVTPLRR LTGWNWLVRL RRMLGLYAFF YVFLHFTIFF WLDHFFDFQE MWKDIVKRPF
ITVGVLAFAL LIPLAITSTN AMVRRLGGKR WQWLHRLTYV IVPLGVLHFW WVKAGKNVLA
QPILFATIVA ALLLMRILSQ KNRQQLAQLF SRRDAGAGLV EESK
//
