NQRC_VIBC3
ID NQRC_VIBC3 Reviewed; 257 AA.
AC A5F5Y7; C3M417; Q9X4Q5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
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:11888296};
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:11888296};
GN OrderedLocusNames=VC0395_A1882, VC395_2409;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10077658; DOI=10.1073/pnas.96.6.3183;
RA Haese C.C., Mekalanos J.J.;
RT "Effects of changes in membrane sodium flux on virulence gene expression in
RT Vibrio cholerae.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3183-3187(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
RN [4]
RP COFACTOR, AND MUTAGENESIS OF HIS-216 AND THR-225.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=11248234; DOI=10.1016/s0014-5793(01)02224-4;
RA Barquera B., Haese C.C., Gennis R.B.;
RT "Expression and mutagenesis of the NqrC subunit of the NQR respiratory
RT Na(+) pump from Vibrio cholerae with covalently attached FMN.";
RL FEBS Lett. 492:45-49(2001).
RN [5]
RP CATALYTIC ACTIVITY, SUBUNIT, AND COFACTOR.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=11888296; DOI=10.1021/bi011873o;
RA Barquera B., Hellwig P., Zhou W., Morgan J.E., Haese C.C., Gosink K.K.,
RA Nilges M., Bruesehoff P.J., Roth A., Lancaster C.R., Gennis R.B.;
RT "Purification and characterization of the recombinant Na(+)-translocating
RT NADH:quinone oxidoreductase from Vibrio cholerae.";
RL Biochemistry 41:3781-3789(2002).
RN [6]
RP SUBUNIT.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=20558724; DOI=10.1074/jbc.m109.071126;
RA Casutt M.S., Huber T., Brunisholz R., Tao M., Fritz G., Steuber J.;
RT "Localization and function of the membrane-bound riboflavin in the Na+-
RT translocating NADH:quinone oxidoreductase (Na+-NQR) from Vibrio cholerae.";
RL J. Biol. Chem. 285:27088-27099(2010).
RN [7]
RP COFACTOR, AND PROSTHETIC GROUP AT THR-225.
RX PubMed=22366169; DOI=10.1016/j.bbabio.2012.02.012;
RA Casutt M.S., Schlosser A., Buckel W., Steuber J.;
RT "The single NqrB and NqrC subunits in the Na(+)-translocating NADH: quinone
RT oxidoreductase (Na(+)-NQR) from Vibrio cholerae each carry one covalently
RT attached FMN.";
RL Biochim. Biophys. Acta 1817:1817-1822(2012).
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 -!- 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:11888296};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00427,
CC ECO:0000269|PubMed:11248234, ECO:0000269|PubMed:11888296,
CC ECO:0000269|PubMed:22366169};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00427, ECO:0000269|PubMed:11888296,
CC ECO:0000269|PubMed:20558724}.
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; AF117331; AAD29964.1; -; Genomic_DNA.
DR EMBL; CP000627; ABQ20333.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10399.1; -; Genomic_DNA.
DR RefSeq; WP_000157902.1; NZ_JAACZH010000008.1.
DR PDB; 4U9S; X-ray; 1.70 A; C=44-257.
DR PDBsum; 4U9S; -.
DR AlphaFoldDB; A5F5Y7; -.
DR SMR; A5F5Y7; -.
DR STRING; 345073.VC395_2409; -.
DR EnsemblBacteria; ABQ20333; ABQ20333; VC0395_A1882.
DR GeneID; 57740914; -.
DR KEGG; vco:VC0395_A1882; -.
DR KEGG; vcr:VC395_2409; -.
DR PATRIC; fig|345073.21.peg.2322; -.
DR eggNOG; COG2869; Bacteria.
DR HOGENOM; CLU_077882_0_1_6; -.
DR OMA; GLWDAIW; -.
DR BRENDA; 7.2.1.1; 15862.
DR Proteomes; UP000000249; Chromosome 2.
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; IDA:UniProtKB.
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 3D-structure; Cell inner membrane; Cell membrane; Flavoprotein; FMN;
KW Ion transport; Membrane; NAD; Phosphoprotein; Sodium; Sodium transport;
KW Translocase; Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q56582"
FT CHAIN 2..257
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT C"
FT /id="PRO_0000321863"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
FT MOD_RES 225
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427,
FT ECO:0000269|PubMed:22366169"
FT MUTAGEN 216
FT /note="H->L: Decrease in FMN binding."
FT /evidence="ECO:0000269|PubMed:11248234"
FT MUTAGEN 225
FT /note="T->L: Loss of FMN binding."
FT /evidence="ECO:0000269|PubMed:11248234"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:4U9S"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:4U9S"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:4U9S"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:4U9S"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:4U9S"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:4U9S"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4U9S"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4U9S"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:4U9S"
FT STRAND 117..129
FT /evidence="ECO:0007829|PDB:4U9S"
FT STRAND 132..143
FT /evidence="ECO:0007829|PDB:4U9S"
FT STRAND 145..156
FT /evidence="ECO:0007829|PDB:4U9S"
FT STRAND 159..169
FT /evidence="ECO:0007829|PDB:4U9S"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:4U9S"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:4U9S"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:4U9S"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:4U9S"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4U9S"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:4U9S"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:4U9S"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:4U9S"
FT TURN 241..244
FT /evidence="ECO:0007829|PDB:4U9S"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:4U9S"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:4U9S"
SQ SEQUENCE 257 AA; 27619 MW; 007C09F4FEA4C272 CRC64;
MASNNDSIKK TLFVVIALSL VCSIIVSAAA VGLRDKQKEN AALDKQSKIL QVAGIEAKGS
KQIVELFNKS IEPRLVDFNT GDFVEGDAAN YDQRKAAKEA SESIKLTAEQ DKAKIQRRAN
VGVVYLVKDG DKTSKVILPV HGNGLWSMMY AFVAVETDGN TVSGLTYYEQ GETPGLGGEV
ENPAWRAQWV GKKLFDENHK PAIKIVKGGA PQGSEHGVDG LSGATLTSNG VQNTFDFWLG
DMGFGPFLTK VRDGGLN
