NQRB_VIBAL
ID NQRB_VIBAL Reviewed; 414 AA.
AC Q56587;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit B {ECO:0000255|HAMAP-Rule:MF_00426, ECO:0000303|PubMed:9490015};
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:9490015};
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:7805867};
GN Synonyms=nqr2 {ECO:0000303|PubMed:9490015};
OS Vibrio alginolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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].
RA Hayashi M., Unemoto T., Sugiyama A.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-7 AND 227-238, 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 [5]
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 [6]
RP COFACTOR, PROSTHETIC GROUP AT THR-236, 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 [7]
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 [8]
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_00426,
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_00426, ECO:0000269|PubMed:9490015};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00426,
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_00426, ECO:0000269|PubMed:9490015}.
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=CAA85477.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z37111; CAA85477.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB008030; BAA22911.1; -; Genomic_DNA.
DR PIR; S51016; S51016.
DR AlphaFoldDB; Q56587; -.
DR SMR; Q56587; -.
DR STRING; 663.BAU10_10835; -.
DR TCDB; 3.D.5.1.1; the na(+)-translocating nadh:quinone dehydrogenase (na-ndh or nqr) family.
DR eggNOG; COG1805; 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:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-UniRule.
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; 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:9490015"
FT CHAIN 2..414
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT B"
FT /id="PRO_0000074442"
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 268..288
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:11163785"
FT CONFLICT 229
FT /note="A -> V (in Ref. 1; CAA85477)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="W -> G (in Ref. 1; CAA85477)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 45342 MW; 56A9D46B6579C89A CRC64;
MALKKFLEDI EHHFEPGGKH EKWFALYEAV ATVFYTPGIV TNKSSHVRDS VDLKRIMIMV
WFAVFPAMFW GMYNAGGQAI AALNHMYAGD QLATVISGNW HYWLTEMLGG TIAADAGVGS
KMLLGATYFL PIYATVFLVG GFWEVLFCMV RKHEVNEGFF VTSILFALIV PPTLPLWQAA
LGITFGVVVA KEIFGGTGRN FLNPALAGRA FLFFAYPAQI SGDVVWTAAD GFSGATALSQ
WAQGGNGALV NTVTGSPITW MDAFIGNIPG SIGEVSTLAL MIGAAMIVYM RIASWRIIAG
VMIGMIAVST LFNVIGSDTN PMFNMPWHWH LVLGGFAFGM FFMATDPVSA SFTNKGKWWY
GILIGAMCVM IRVVNPAYPE GMMLAILFAN LFAPLFDHVV IEKNIKRRLA RYGK
