MSRQ_CROS8
ID MSRQ_CROS8 Reviewed; 200 AA.
AC A7MNR0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=ESA_03642;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000783; ABU78852.1; -; Genomic_DNA.
DR RefSeq; WP_012125992.1; NC_009778.1.
DR AlphaFoldDB; A7MNR0; -.
DR SMR; A7MNR0; -.
DR EnsemblBacteria; ABU78852; ABU78852; ESA_03642.
DR KEGG; esa:ESA_03642; -.
DR PATRIC; fig|290339.8.peg.3246; -.
DR HOGENOM; CLU_080662_1_0_6; -.
DR OMA; LHFFWMR; -.
DR OrthoDB; 1508607at2; -.
DR Proteomes; UP000000260; 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; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..200
FT /note="Protein-methionine-sulfoxide reductase heme-binding
FT subunit MsrQ"
FT /id="PRO_1000085529"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01207"
SQ SEQUENCE 200 AA; 22992 MW; 0258757EBBB66C05 CRC64;
MRLTAKQITW LKVALHLAAF LPLVWLFYAA SQGLFRADPA KDIQHFTGRM ALKLLLATLL
VTPLTRLLKQ PLLIRTRRLL GLWCFAWATL HLVSYSLLEL GLSNLSLLGS ELVSRPYLTL
GIVSWLILLA LALTSFQAAQ RKLGRRWQTL HNFIYLVAIL APIHYLWSVK ILSPQPVLYA
LGAIVLLAWR YKKLRQWWRT
