QRCD_DESVH
ID QRCD_DESVH Reviewed; 419 AA.
AC Q72E86;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Menaquinone reductase, integral membrane subunit {ECO:0000305|PubMed:20498375};
DE AltName: Full=Quinone reductase complex subunit D {ECO:0000303|PubMed:20498375};
DE AltName: Full=Type I cytochrome c3:menaquinone oxidoreductase subunit D {ECO:0000303|PubMed:20498375};
GN Name=qrcD {ECO:0000303|PubMed:20498375};
GN OrderedLocusNames=DVU_0692 {ECO:0000312|EMBL:AAS95173.1};
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=20498375; DOI=10.1074/jbc.m110.124305;
RA Venceslau S.S., Lino R.R., Pereira I.A.;
RT "The Qrc membrane complex, related to the alternative complex III, is a
RT menaquinone reductase involved in sulfate respiration.";
RL J. Biol. Chem. 285:22774-22783(2010).
RN [3]
RP INTERACTION WITH [NIFE] HYDROGENASE AND TPIC(3).
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=21651911; DOI=10.1016/j.febslet.2011.05.054;
RA Venceslau S.S., Matos D., Pereira I.A.;
RT "EPR characterization of the new Qrc complex from sulfate reducing bacteria
RT and its ability to form a supercomplex with hydrogenase and TpIc3.";
RL FEBS Lett. 585:2177-2181(2011).
CC -!- FUNCTION: Component of the respiratory Qrc complex, that catalyzes the
CC reduction of the menaquinone pool using electrons transferred from the
CC reduced periplasmic cytochrome c3, and which is probably involved in
CC sulfate respiration. Is likely essential for growth on H(2) or formate
CC since the periplasmic hydrogenases and/or formate dehydrogenases act as
CC primary electron donors for the Qrc complex. The QrcD subunit anchors
CC the protein complex to the membrane and likely interacts with the
CC quinone pool. {ECO:0000269|PubMed:20498375}.
CC -!- SUBUNIT: The Qrc complex is composed of four subunits: QrcA, QrcB, QrcC
CC and QrcD (PubMed:20498375). Can form a supercomplex with the [NiFe]
CC hydrogenase HynA1 and the tetraheme Type I cytochrome c3 TpIc(3), its
CC physiological electron donors (PubMed:21651911).
CC {ECO:0000269|PubMed:20498375, ECO:0000269|PubMed:21651911}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:20498375}; Multi-pass membrane protein
CC {ECO:0000255, ECO:0000305|PubMed:20498375}.
CC -!- SIMILARITY: Belongs to the NrfD family. {ECO:0000305}.
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DR EMBL; AE017285; AAS95173.1; -; Genomic_DNA.
DR RefSeq; WP_010937995.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_009914.1; NC_002937.3.
DR AlphaFoldDB; Q72E86; -.
DR SMR; Q72E86; -.
DR STRING; 882.DVU_0692; -.
DR PaxDb; Q72E86; -.
DR EnsemblBacteria; AAS95173; AAS95173; DVU_0692.
DR KEGG; dvu:DVU_0692; -.
DR PATRIC; fig|882.5.peg.648; -.
DR eggNOG; COG5557; Bacteria.
DR HOGENOM; CLU_049007_0_0_7; -.
DR OMA; FGYWHPN; -.
DR PhylomeDB; Q72E86; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009061; P:anaerobic respiration; IEA:UniProtKB-KW.
DR InterPro; IPR005614; NrfD_fam.
DR Pfam; PF03916; NrfD; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Electron transport; Membrane; Reference proteome; Sulfate respiration;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..419
FT /note="Menaquinone reductase, integral membrane subunit"
FT /id="PRO_0000438001"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 419 AA; 47537 MW; 141AE02F46ACADC8 CRC64;
MDKNYNLPVD AELFPEGCER CSLSKFMMWM AFVFVFFGWG LYAAYRVLAE GLGVTGLDDY
FGFGLWITFD LAVIALGAGA FFSGLLRYIL NIDPLKNIIN LAVIIGFLCY SGAMLVLVLD
IGQPLRAWFG YWHANVHSML TEVIFCITCY CLVLIIEYVP LILENRQLNK NKLVHAVAHN
FHVMMPLFAG IGAFLSTFHQ GSLGGMYGVL FGRPYIYREG FFIWPWTFFL YVLSAVGSGP
VFTVLVCTLM EKMTGRKLVS WEVKSLMGKI AGTMLMVYLI FKFADTYAWA YDLLPRQGLT
FDQMFTSGWI YGKWMLWAEL FYCGLVPAII LIVPALRNNP VLFYSAAILD CIGITINRYV
MTVQALAIPV MPFDSWESYL PNWAEWGASV MIVAYAALVL SLSYRYLPIF PQEAELNRK
