QRCB_DESVH
ID QRCB_DESVH Reviewed; 691 AA.
AC Q72E84;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Menaquinone reductase, molybdopterin-binding-like subunit {ECO:0000305|PubMed:20498375};
DE AltName: Full=Quinone reductase complex subunit B {ECO:0000303|PubMed:20498375};
DE AltName: Full=Type I cytochrome c3:menaquinone oxidoreductase subunit B {ECO:0000303|PubMed:20498375};
DE Flags: Precursor;
GN Name=qrcB {ECO:0000303|PubMed:20498375};
GN OrderedLocusNames=DVU_0694 {ECO:0000312|EMBL:AAS95175.1};
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, COFACTOR,
RP SUBUNIT, AND 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 function of the QrcB
CC subunit is unknown; in the absence of a catalytic site, it may provide
CC a structural scaffold for the other subunits.
CC {ECO:0000269|PubMed:20498375}.
CC -!- COFACTOR:
CC Note=There is no molybdenum or tungsten pterin cofactor present in the
CC Qrc complex, despite the similarity of QrcB to molybdopterin-containing
CC oxidoreductases. {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 -!- INTERACTION:
CC Q72E84; Q72E85: qrcC; NbExp=2; IntAct=EBI-6974672, EBI-10070807;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:20498375}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE017285; AAS95175.1; -; Genomic_DNA.
DR RefSeq; WP_010937997.1; NC_002937.3.
DR RefSeq; YP_009916.1; NC_002937.3.
DR AlphaFoldDB; Q72E84; -.
DR SMR; Q72E84; -.
DR IntAct; Q72E84; 2.
DR MINT; Q72E84; -.
DR STRING; 882.DVU_0694; -.
DR PaxDb; Q72E84; -.
DR PRIDE; Q72E84; -.
DR EnsemblBacteria; AAS95175; AAS95175; DVU_0694.
DR KEGG; dvu:DVU_0694; -.
DR PATRIC; fig|882.5.peg.650; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_7; -.
DR OMA; QNWPWIP; -.
DR PhylomeDB; Q72E84; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IEA:UniProtKB-KW.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Molybdenum; Oxidoreductase; Periplasm; Reference proteome;
KW Signal; Sulfate respiration; Transport.
FT SIGNAL 1..27
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 28..691
FT /note="Menaquinone reductase, molybdopterin-binding-like
FT subunit"
FT /id="PRO_0000437999"
FT DOMAIN 50..106
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
SQ SEQUENCE 691 AA; 72355 MW; F0E5C3EFEDC810FF CRC64;
MALDRRGFLK FIGGATAGIL ATPVVWKGLD DVSIWSQNWS WIPRNIKGAN SYVPTVSKLC
PTGIGVRVRL VDGRPVRVIG NPEHPLSKGG VSSIAAAEVQ MLYSPARMKR PLKRSPDGAY
VMISWEEAEA MLLDGLKAAK GGDALACISG DDNGTINELL SAFVQQSGSK SFFLMPGEAQ
PAAKAWDLMG GEGQIGYDIE KSDFVLAIGA NVLEAWGTAI RNRHAFGASH PHGAEPTAQF
VYAGPVLNNT ATGADDWLPI RPGTESAFAL GLAHLLIKAG ASSSAPDFDA FRSLAASFSP
EKVAAQTGVD AKALTALAQA LAKAKHPLVI VGSEFSQGAG AAPVMAGIAL NMLLGSVNRD
GGLRALPVAR KVVPAGMDRK AMLQQDLTLW ASAIASGKAK APKAMLVYEA NPVYALPQGS
AFKDTLAKVP FKVAFTSFLD ETAMQCDLVI PVSMGLERLD DVCTPYGCGE VVYSLATPVT
APLFDTKPAG DALIALGGKL GLDLGVASFE DMLKAKAAAH GADFDKLAEG TAFTSRATVG
ANLSFRPDVL SKALDVKAPA LPLALAPVMK LNMGTSKTAI PPFNTKTIRR WEVQGKEGYV
MLNGATARKL GLAQHDRVVL SNPTGKVTVR VNIFEGVMND TVAMPLGFGH TAFDEFSKGK
GENVMHLLAP STEPVTGLAV WTGAGVNIAK A
