NQRC_VIBAL
ID NQRC_VIBAL Reviewed; 256 AA.
AC Q56582; Q56566; Q56588;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit C {ECO:0000255|HAMAP-Rule:MF_00427, ECO:0000303|PubMed:9490015};
DE Short=Na(+)-NQR subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
DE Short=Na(+)-translocating NQR subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
DE EC=7.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00427, ECO:0000269|PubMed:9490015};
DE AltName: Full=NQR complex subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
DE AltName: Full=NQR-1 subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
GN Name=nqrC {ECO:0000255|HAMAP-Rule:MF_00427, ECO:0000303|PubMed:7805867};
GN Synonyms=nqr3 {ECO:0000303|PubMed:7729558};
OS Vibrio alginolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC STRAIN=NCIMB 11038 / LMG 3418;
RX PubMed=7805867; DOI=10.1016/0014-5793(94)01275-x;
RA Beattie P., Tan K., Bourne R.M., Leach D.R.F., Rich P.R., Ward F.B.;
RT "Cloning and sequencing of four structural genes for the Na(+)-
RT translocating NADH-ubiquinone oxidoreductase of Vibrio alginolyticus.";
RL FEBS Lett. 356:333-338(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7729558; DOI=10.1016/0014-5793(95)00283-f;
RA Hayashi M., Hirai K., Unemoto T.;
RT "Sequencing and the alignment of structural genes in the nqr operon
RT encoding the Na(+)-translocating NADH-quinone reductase from Vibrio
RT alginolyticus.";
RL FEBS Lett. 363:75-77(1995).
RN [3]
RP PROTEIN SEQUENCE OF 2-12 AND 171-177.
RX PubMed=7805866; DOI=10.1016/0014-5793(94)01274-1;
RA Hayashi M., Hirai K., Unemoto T.;
RT "Cloning of the Na(+)-translocating NADH-quinone reductase gene from the
RT marine bacterium Vibrio alginolyticus and the expression of the beta-
RT subunit in Escherichia coli.";
RL FEBS Lett. 356:330-332(1994).
RN [4]
RP PROTEIN SEQUENCE OF 2-11, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=9490015; DOI=10.1016/s0014-5793(98)00016-7;
RA Nakayama Y., Hayashi M., Unemoto T.;
RT "Identification of six subunits constituting Na+-translocating NADH-quinone
RT reductase from the marine Vibrio alginolyticus.";
RL FEBS Lett. 422:240-242(1998).
RN [5]
RP PROTEIN SEQUENCE OF 2-8 AND 220-229, AND COFACTOR.
RX PubMed=10838078; DOI=10.1016/s0014-5793(00)01595-7;
RA Nakayama Y., Yasui M., Sugahara K., Hayashi M., Unemoto T.;
RT "Covalently bound flavin in the NqrB and NqrC subunits of Na(+)-
RT translocating NADH-quinone reductase from Vibrio alginolyticus.";
RL FEBS Lett. 474:165-168(2000).
RN [6]
RP INHIBITION OF ENZYMATIC ACTIVITY.
RX PubMed=10549856; DOI=10.1248/bpb.22.1064;
RA Nakayama Y., Hayashi M., Yoshikawa K., Mochida K., Unemoto T.;
RT "Inhibitor studies of a new antibiotic, korormicin, 2-n-heptyl-4-
RT hydroxyquinoline N-oxide and Ag+ toward the Na+-translocating NADH-quinone
RT reductase from the marine Vibrio alginolyticus.";
RL Biol. Pharm. Bull. 22:1064-1067(1999).
RN [7]
RP COFACTOR, PROSTHETIC GROUP AT THR-224, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=11163785; DOI=10.1016/s0014-5793(00)02404-2;
RA Hayashi M., Nakayama Y., Yasui M., Maeda M., Furuishi K., Unemoto T.;
RT "FMN is covalently attached to a threonine residue in the NqrB and NqrC
RT subunits of Na(+)-translocating NADH-quinone reductase from Vibrio
RT alginolyticus.";
RL FEBS Lett. 488:5-8(2001).
RN [8]
RP REVIEW.
RX PubMed=11248187; DOI=10.1016/s0005-2728(00)00275-9;
RA Hayashi M., Nakayama Y., Unemoto T.;
RT "Recent progress in the Na(+)-translocating NADH-quinone reductase from the
RT marine Vibrio alginolyticus.";
RL Biochim. Biophys. Acta 1505:37-44(2001).
RN [9]
RP REVIEW.
RX PubMed=11248188; DOI=10.1016/s0005-2728(00)00276-0;
RA Steuber J.;
RT "Na(+) translocation by bacterial NADH:quinone oxidoreductases: an
RT extension to the complex-I family of primary redox pumps.";
RL Biochim. Biophys. Acta 1505:45-56(2001).
CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to
CC ubiquinol by two successive reactions, coupled with the transport of
CC Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are
CC probably involved in the second step, the conversion of ubisemiquinone
CC to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00427,
CC ECO:0000305|PubMed:11248187, ECO:0000305|PubMed:11248188}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n
CC Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-COMP:9565,
CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389,
CC ChEBI:CHEBI:17976, ChEBI:CHEBI:29101, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=7.2.1.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00427, ECO:0000269|PubMed:9490015};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00427,
CC ECO:0000269|PubMed:10838078, ECO:0000269|PubMed:11163785};
CC -!- ACTIVITY REGULATION: This reaction is tightly coupled to the Na(+)
CC pumping activity and specifically requires Na(+) for activity.
CC Inhibited by korormicin and 2-N-heptyl-4-hydroxyquinoline N-oxide
CC (HQNO). {ECO:0000269|PubMed:10549856}.
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00427, ECO:0000269|PubMed:9490015}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00427, ECO:0000305}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00427}.
CC -!- SIMILARITY: Belongs to the NqrC family. {ECO:0000255|HAMAP-
CC Rule:MF_00427, ECO:0000305}.
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DR EMBL; Z37111; CAA85478.1; -; Genomic_DNA.
DR EMBL; AB008030; BAA22912.1; -; Genomic_DNA.
DR PIR; S65528; S65528.
DR AlphaFoldDB; Q56582; -.
DR SMR; Q56582; -.
DR STRING; 663.BAU10_10830; -.
DR TCDB; 3.D.5.1.1; the na(+)-translocating nadh:quinone dehydrogenase (na-ndh or nqr) family.
DR eggNOG; COG2869; Bacteria.
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:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IDA:UniProtKB.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00427; NqrC; 1.
DR InterPro; IPR007329; FMN-bd.
DR InterPro; IPR010204; NqrC.
DR PANTHER; PTHR37838; PTHR37838; 1.
DR Pfam; PF04205; FMN_bind; 1.
DR PIRSF; PIRSF009437; NQR-1_subunit_C; 1.
DR SMART; SM00900; FMN_bind; 1.
DR TIGRFAMs; TIGR01938; nqrC; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Flavoprotein; FMN; Ion transport; Membrane; NAD; Phosphoprotein; Sodium;
KW Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10838078,
FT ECO:0000269|PubMed:7805866, ECO:0000269|PubMed:7805867,
FT ECO:0000269|PubMed:9490015"
FT CHAIN 2..256
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT C"
FT /id="PRO_0000214221"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
FT MOD_RES 224
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427,
FT ECO:0000269|PubMed:11163785"
FT CONFLICT 184
FT /note="W -> R (in Ref. 1; CAA85478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 256 AA; 27703 MW; 150DCD862BCB7CE7 CRC64;
MASNNDSIKK TLGVVIGLSL VCSIIVSTAA VGLRDKQKAN AVLDKQSKIV EVAGIDANGK
KVPELFAEYI EPRLVDLETG NFTEGNASTY DQREASKDAE RSIALTPEED VADIRRRANT
AVVYLVKDQD EVQKVILPMH GKGLWSMMYA FVAVETDGNT VSAITYYEQG ETPGLGGEVE
NPSWRDQFIG KKLYNEDHQP AIKVVKGGAP QGSEHGVDGL SGATLTSNGV QHTFDFWLGD
KGFGPFLAKV RDGELN
