MSRQ_RHIME
ID MSRQ_RHIME Reviewed; 216 AA.
AC Q92QE8;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ {ECO:0000255|HAMAP-Rule:MF_01207};
DE AltName: Full=Flavocytochrome MsrQ {ECO:0000255|HAMAP-Rule:MF_01207};
GN Name=msrQ {ECO:0000255|HAMAP-Rule:MF_01207}; OrderedLocusNames=R01382;
GN ORFNames=SMc01282;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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:0000255|HAMAP-Rule:MF_01207}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01207};
CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_01207};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01207};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01207};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-binding
CC subunit (MsrQ). {ECO:0000255|HAMAP-Rule:MF_01207}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01207}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01207}.
CC -!- SIMILARITY: Belongs to the MsrQ family. {ECO:0000255|HAMAP-
CC Rule:MF_01207}.
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DR EMBL; AL591688; CAC45961.1; -; Genomic_DNA.
DR RefSeq; NP_385488.1; NC_003047.1.
DR RefSeq; WP_010969198.1; NC_003047.1.
DR AlphaFoldDB; Q92QE8; -.
DR STRING; 266834.SMc01282; -.
DR EnsemblBacteria; CAC45961; CAC45961; SMc01282.
DR GeneID; 61602844; -.
DR KEGG; sme:SMc01282; -.
DR PATRIC; fig|266834.11.peg.2799; -.
DR eggNOG; COG2717; Bacteria.
DR HOGENOM; CLU_080662_2_0_5; -.
DR OMA; LHFFWMR; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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; PTHR36964; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; Flavoprotein; FMN;
KW Heme; Iron; Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..216
FT /note="Protein-methionine-sulfoxide reductase heme-binding
FT subunit MsrQ"
FT /id="PRO_0000091582"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
SQ SEQUENCE 216 AA; 24592 MW; 68C7FCE7E5930C42 CRC64;
MRSLPALPKR LHGPSIWALY ILGFLPAVWG FYLGATGRLP GNAVKEFEHL LGIWALRFLI
ATLAITPIRD LFGVNWLRYR RALGLLAFYY VMMHFLTYMV LDQTLLLPAI VADIARRPFI
TIGMAALVLL IPLAVTSNIW SIRRLGQRWN KLHRLVYVIA AAGALHFAMS VKVVGPEQML
YLFLVAVLVA WRAVRKRFLR WRRQGTAPMR SQARAG
