QRCC_DESVH
ID QRCC_DESVH Reviewed; 255 AA.
AC Q72E85;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Menaquinone reductase, iron-sulfur cluster-binding subunit {ECO:0000305|PubMed:20498375};
DE EC=1.97.-.-;
DE AltName: Full=Quinone reductase complex subunit C {ECO:0000303|PubMed:20498375};
DE AltName: Full=Type I cytochrome c3:menaquinone oxidoreductase subunit C {ECO:0000303|PubMed:20498375};
GN Name=qrcC {ECO:0000303|PubMed:20498375};
GN OrderedLocusNames=DVU_0693 {ECO:0000312|EMBL:AAS95174.1};
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 2-7, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, 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), AND COFACTOR.
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. QrcC is an electron-
CC transferring subunit; its cubane iron sulfur clusters form a pathway
CC for electron transfer between the hemes of QrcA and the membrane
CC quinone pool. {ECO:0000269|PubMed:20498375}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:20498375, ECO:0000269|PubMed:21651911};
CC Note=Binds 3 [4Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:20498375, ECO:0000269|PubMed:21651911};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000269|PubMed:20498375, ECO:0000269|PubMed:21651911};
CC Note=Binds 1 [3Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:20498375, ECO:0000269|PubMed:21651911};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 uM for the cytochrome c3 {ECO:0000269|PubMed:20498375};
CC KM=4.0 uM for menaquinone-4 {ECO:0000269|PubMed:20498375};
CC Vmax=92 nmol/min/mg enzyme {ECO:0000269|PubMed:20498375};
CC Note=kcat is 16.6 min(-1). Values are measured with the whole Qrc
CC complex. {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 Q72E85; Q72E84: qrcB; NbExp=2; IntAct=EBI-10070807, EBI-6974672;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:20498375}.
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DR EMBL; AE017285; AAS95174.1; -; Genomic_DNA.
DR RefSeq; WP_010937996.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_009915.1; NC_002937.3.
DR AlphaFoldDB; Q72E85; -.
DR SMR; Q72E85; -.
DR IntAct; Q72E85; 1.
DR STRING; 882.DVU_0693; -.
DR PaxDb; Q72E85; -.
DR EnsemblBacteria; AAS95174; AAS95174; DVU_0693.
DR KEGG; dvu:DVU_0693; -.
DR PATRIC; fig|882.5.peg.649; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_043374_1_0_7; -.
DR OMA; EKCTWCY; -.
DR PhylomeDB; Q72E85; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF13247; Fer4_11; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 1: Evidence at protein level;
KW 3Fe-4S; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Oxidoreductase; Periplasm; Reference proteome;
KW Sulfate respiration; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:20498375"
FT CHAIN 2..255
FT /note="Menaquinone reductase, iron-sulfur cluster-binding
FT subunit"
FT /id="PRO_0000438000"
FT DOMAIN 11..41
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 66..97
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 99..128
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 30
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 78
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 108
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 155
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000305"
FT BINDING 158
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000305"
FT BINDING 188
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000305"
FT BINDING 192
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 29043 MW; 4FE7CC9F3CA5C426 CRC64;
MSSFKEFKIK WGMVIDLDKC TGCGACMVAC QAENNIAPQP DASNKLKSLN WLVVYELNNG
KPFPEHDVAY LPRPCMQCGK PSCVSVCPVV ATDKNEEGGI VSQVYPRCIG CRYCMASCPY
HARYFNWFDP TWPEGMDKTL TPDVSVRPRG VVEKCTFCHH RFMQAKDKAR VEGRDPSALR
DGDYVTSCTE ACPNGAIIFG DFNNPEHRVH ELHKSKYAFR LLERLGTDPQ VYYLSRREWV
RRLGDNYLEH EKVKG
