NQRB_VIBC1
ID NQRB_VIBC1 Reviewed; 413 AA.
AC Q9RFW0; A7N1U5;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
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};
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};
GN OrderedLocusNames=VIBHAR_03274;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10587447; DOI=10.1021/bi991664s;
RA Zhou W., Bertsova Y.V., Feng B., Tsatsos P., Verkhovskaya M.L.,
RA Gennis R.B., Bogachev A.V., Barquera B.;
RT "Sequencing and preliminary characterization of the Na+-translocating
RT NADH:ubiquinone oxidoreductase from Vibrio harveyi.";
RL Biochemistry 38:16246-16252(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00426};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00426}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00426}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00426}.
CC -!- SIMILARITY: Belongs to the NqrB/RnfD family. {ECO:0000255|HAMAP-
CC Rule:MF_00426}.
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DR EMBL; AF165980; AAF15412.1; -; Genomic_DNA.
DR EMBL; CP000789; ABU72222.1; -; Genomic_DNA.
DR RefSeq; WP_012128722.1; NC_022269.1.
DR AlphaFoldDB; Q9RFW0; -.
DR SMR; Q9RFW0; -.
DR EnsemblBacteria; ABU72222; ABU72222; VIBHAR_03274.
DR KEGG; vha:VIBHAR_03274; -.
DR PATRIC; fig|338187.25.peg.2918; -.
DR OMA; FNPAYPE; -.
DR OrthoDB; 1654433at2; -.
DR Proteomes; UP000008152; Chromosome I.
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; IEA:InterPro.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
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..413
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT B"
FT /id="PRO_0000074445"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT MOD_RES 235
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT CONFLICT 243
FT /note="G -> R (in Ref. 1; AAF15412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 45252 MW; 44558479BCF4516B CRC64;
MLKKFIEDIE HHFEPGGKHE KWFALYEAAA TLFYTPGLVT KRSSHVRDSV DLKRIMIMVW
FAVFPAMFWG MYNAGGQAIA ALNHMYAGDQ LATVIAGNWH YWLTEMLGGT IGAEAGVGSM
MLLGATYFLP IYATVFIVGG FWEVLFCMVR KHEVNEGFFV TSILFALIVP PTLPLWQAAL
GITFGVVVAK EIFGGTGRNF LNPALAGRAF LFFAYPAQIS GDVVWTAADG FSGATALSQW
AHGGSGALIN NITGAPITWM DAFIGNIPGS IGEVSTLALM IGAAMIVYMR IASWRIIAGV
MIGMIAVSTL FNVIGSDTNP MFNMPWHWHL VLGGFAFGMF FMATDPVSAS FTNSGKWWYG
ILIGAMCVMI RVVNPAYPEG MMLAILFANL FAPLFDHVVI EKNIKRRLAR YGK
