NQRB_VIBC3
ID NQRB_VIBC3 Reviewed; 415 AA.
AC A5F5X0; C3M418;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit B {ECO:0000255|HAMAP-Rule:MF_00426};
DE Short=Na(+)-NQR subunit B {ECO:0000255|HAMAP-Rule:MF_00426};
DE Short=Na(+)-translocating NQR subunit B {ECO:0000255|HAMAP-Rule:MF_00426};
DE EC=7.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00426, ECO:0000269|PubMed:11888296};
DE AltName: Full=NQR complex subunit B {ECO:0000255|HAMAP-Rule:MF_00426};
DE AltName: Full=NQR-1 subunit B {ECO:0000255|HAMAP-Rule:MF_00426};
GN Name=nqrB {ECO:0000255|HAMAP-Rule:MF_00426, ECO:0000303|PubMed:11888296};
GN OrderedLocusNames=VC0395_A1883 {ECO:0000312|EMBL:ABQ21010.1},
GN VC395_2410 {ECO:0000312|EMBL:ACP10400.1};
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 [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 [2]
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 [3]
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 [4]
RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF PHE-185 AND TRP-226.
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 [5]
RP COFACTOR, AND PROSTHETIC GROUP AT THR-236.
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_00426}.
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_00426, ECO:0000269|PubMed:11888296};
CC -!- COFACTOR:
CC Name=riboflavin; Xref=ChEBI:CHEBI:57986;
CC Evidence={ECO:0000269|PubMed:20558724};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00426,
CC ECO:0000269|PubMed:11888296, ECO:0000269|PubMed:20558724,
CC ECO:0000269|PubMed:22366169};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00426, ECO:0000269|PubMed:11888296,
CC ECO:0000269|PubMed:20558724}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00426, ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00426}.
CC -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000255|HAMAP-
CC Rule:MF_00426, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACP10400.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000627; ABQ21010.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10400.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000523294.1; NZ_JAACZH010000008.1.
DR AlphaFoldDB; A5F5X0; -.
DR SMR; A5F5X0; -.
DR STRING; 345073.VC395_2410; -.
DR EnsemblBacteria; ABQ21010; ABQ21010; VC0395_A1883.
DR GeneID; 57740915; -.
DR GeneID; 66939858; -.
DR KEGG; vco:VC0395_A1883; -.
DR KEGG; vcr:VC395_2410; -.
DR PATRIC; fig|345073.21.peg.2323; -.
DR eggNOG; COG1805; Bacteria.
DR HOGENOM; CLU_042020_1_1_6; -.
DR OMA; FNPAYPE; -.
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:1902444; F:riboflavin binding; IDA:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR HAMAP; MF_00426; NqrB; 1.
DR InterPro; IPR010966; NqrB.
DR InterPro; IPR004338; NqrB/RnfD.
DR PANTHER; PTHR30578; PTHR30578; 1.
DR Pfam; PF03116; NQR2_RnfD_RnfE; 1.
DR PIRSF; PIRSF016055; NADH-UbQ_OxRdtase_B_su; 1.
DR TIGRFAMs; TIGR01937; nqrB; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Flavoprotein; FMN; Ion transport;
KW Membrane; NAD; Phosphoprotein; Sodium; Sodium transport; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..415
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT B"
FT /id="PRO_0000431655"
FT TRANSMEM 23..40
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT MOD_RES 236
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426,
FT ECO:0000269|PubMed:22366169"
FT MUTAGEN 185
FT /note="F->A: Decreases riboflavin content."
FT /evidence="ECO:0000269|PubMed:20558724"
FT MUTAGEN 226
FT /note="W->L: Decreases riboflavin content."
FT /evidence="ECO:0000269|PubMed:20558724"
SQ SEQUENCE 415 AA; 45357 MW; 8DF4F1FD6DAE8DAF CRC64;
MGLKKFLEDI EHHFEPGGKH EKWFALYEAA ATLFYTPGLV TKRSSHVRDS VDLKRIMIMV
WLAVFPAMFW GMYNAGGQAI AALNHLYSGD QLAAIVAGNW HYWLTEMLGG TMSSDAGWGS
KMLLGATYFL PIYATVFIVG GFWEVLFCMV RKHEVNEGFF VTSILFALIV PPTLPLWQAA
LGITFGVVVA KEVFGGTGRN FLNPALAGRA FLFFAYPAQI SGDLVWTAAD GYSGATALSQ
WAQGGAGALI NNATGQTITW MDAFIGNIPG SIGEVSTLAL MIGAAFIVYM GIASWRIIGG
VMIGMILLST LFNVIGSDTN AMFNMPWHWH LVLGGFAFGM FFMATDPVSA SFTNSGKWAY
GILIGVMCVL IRVVNPAYPE GMMLAILFAN LFAPLFDHVV VERNIKRRLA RYGKQ
