MSRQ_ECOLI
ID MSRQ_ECOLI Reviewed; 211 AA.
AC P76343; Q2MAZ6;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ {ECO:0000255|HAMAP-Rule:MF_01207, ECO:0000305|PubMed:26641313};
DE AltName: Full=Flavocytochrome MsrQ {ECO:0000255|HAMAP-Rule:MF_01207};
GN Name=msrQ {ECO:0000303|PubMed:26641313};
GN Synonyms=yedZ {ECO:0000312|EMBL:AAC75038.1};
GN OrderedLocusNames=b1972, JW1955;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP TOPOLOGY.
RX PubMed=11867724; DOI=10.1073/pnas.052018199;
RA Drew D., Sjoestrand D., Nilsson J., Urbig T., Chin C.-N., de Gier J.-W.,
RA von Heijne G.;
RT "Rapid topology mapping of Escherichia coli inner-membrane proteins by
RT prediction and PhoA/GFP fusion analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2690-2695(2002).
RN [4]
RP COFACTOR, DISRUPTION PHENOTYPE, EPR SPECTROSCOPY, REDOX POTENTIAL,
RP INTERACTION WITH MSRP, AND SUBUNIT.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16042411; DOI=10.1021/bi050621a;
RA Brokx S.J., Rothery R.A., Zhang G., Ng D.P., Weiner J.H.;
RT "Characterization of an Escherichia coli sulfite oxidase homologue reveals
RT the role of a conserved active site cysteine in assembly and function.";
RL Biochemistry 44:10339-10348(2005).
RN [5]
RP COFACTOR, AND FMN-BINDING.
RX PubMed=15987891; DOI=10.1110/ps.051466205;
RA Drew D., Slotboom D.J., Friso G., Reda T., Genevaux P., Rapp M.,
RA Meindl-Beinker N.M., Lambert W., Lerch M., Daley D.O., Van Wijk K.J.,
RA Hirst J., Kunji E., De Gier J.W.;
RT "A scalable, GFP-based pipeline for membrane protein overexpression
RT screening and purification.";
RL Protein Sci. 14:2011-2017(2005).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=26641313; DOI=10.1038/nature15764;
RA Gennaris A., Ezraty B., Henry C., Agrebi R., Vergnes A., Oheix E., Bos J.,
RA Leverrier P., Espinosa L., Szewczyk J., Vertommen D., Iranzo O.,
RA Collet J.F., Barras F.;
RT "Repairing oxidized proteins in the bacterial envelope using respiratory
RT chain electrons.";
RL Nature 528:409-412(2015).
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. MsrPQ is essential for the maintenance of envelope integrity
CC under bleach stress, rescuing a wide series of structurally unrelated
CC periplasmic proteins from methionine oxidation, including the primary
CC periplasmic chaperone SurA and the lipoprotein Pal. MsrQ provides
CC electrons for reduction to the reductase catalytic subunit MsrP, using
CC the quinone pool of the respiratory chain.
CC {ECO:0000269|PubMed:26641313}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:15987891};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:15987891};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:16042411};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000269|PubMed:16042411};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -8 +/-16 mV at pH 7 for heme b.
CC {ECO:0000269|PubMed:16042411};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-binding
CC subunit (MsrQ). {ECO:0000269|PubMed:16042411}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01207, ECO:0000305|PubMed:26641313}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking the msrPQ genes display no visible
CC growth defect. {ECO:0000269|PubMed:16042411}.
CC -!- SIMILARITY: Belongs to the MsrQ family. {ECO:0000255|HAMAP-
CC Rule:MF_01207}.
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DR EMBL; U00096; AAC75038.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76560.1; -; Genomic_DNA.
DR PIR; H64961; H64961.
DR RefSeq; NP_416481.1; NC_000913.3.
DR RefSeq; WP_001240091.1; NZ_LN832404.1.
DR AlphaFoldDB; P76343; -.
DR BioGRID; 4260772; 11.
DR IntAct; P76343; 1.
DR STRING; 511145.b1972; -.
DR PaxDb; P76343; -.
DR PRIDE; P76343; -.
DR EnsemblBacteria; AAC75038; AAC75038; b1972.
DR EnsemblBacteria; BAE76560; BAE76560; BAE76560.
DR GeneID; 66674138; -.
DR GeneID; 946483; -.
DR KEGG; ecj:JW1955; -.
DR KEGG; eco:b1972; -.
DR PATRIC; fig|1411691.4.peg.278; -.
DR EchoBASE; EB3801; -.
DR eggNOG; COG2717; Bacteria.
DR HOGENOM; CLU_080662_1_0_6; -.
DR InParanoid; P76343; -.
DR OMA; LHFFWMR; -.
DR PhylomeDB; P76343; -.
DR BioCyc; EcoCyc:G7060-MON; -.
DR BioCyc; MetaCyc:G7060-MON; -.
DR BRENDA; 1.8.5.B1; 2026.
DR PRO; PR:P76343; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016679; F:oxidoreductase activity, acting on diphenols and related substances as donors; IDA:EcoCyc.
DR GO; GO:0030091; P:protein repair; IDA:UniProtKB.
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 1: Evidence at protein level;
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..211
FT /note="Protein-methionine-sulfoxide reductase heme-binding
FT subunit MsrQ"
FT /id="PRO_0000091574"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TOPO_DOM 31..44
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TOPO_DOM 68..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TOPO_DOM 103..115
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TOPO_DOM 137..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 150..167
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TOPO_DOM 168..170
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..189
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TOPO_DOM 190..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 24068 MW; 4BB07AFF858D69BB CRC64;
MRLTAKQVTW LKVCLHLAGL LPFLWLVWAI NHGGLGADPV KDIQHFTGRT ALKFLLATLL
ITPLARYAKQ PLLIRTRRLL GLWCFAWATL HLTSYALLEL GVNNLALLGK ELITRPYLTL
GIISWVILLA LAFTSTQAMQ RKLGKHWQQL HNFVYLVAIL APIHYLWSVK IISPQPLIYA
GLAVLLLALR YKKLRSLFNR LRKQVHNKLS V
