NQRB_CHRSD
ID NQRB_CHRSD Reviewed; 411 AA.
AC Q1QX85;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 103.
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}; OrderedLocusNames=Csal_1570;
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
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; CP000285; ABE58923.1; -; Genomic_DNA.
DR RefSeq; WP_011506869.1; NC_007963.1.
DR AlphaFoldDB; Q1QX85; -.
DR SMR; Q1QX85; -.
DR STRING; 290398.Csal_1570; -.
DR EnsemblBacteria; ABE58923; ABE58923; Csal_1570.
DR KEGG; csa:Csal_1570; -.
DR eggNOG; COG1805; Bacteria.
DR HOGENOM; CLU_042020_1_1_6; -.
DR OMA; FNPAYPE; -.
DR OrthoDB; 1654433at2; -.
DR Proteomes; UP000000239; Chromosome.
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; Reference proteome; Sodium;
KW Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..411
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT B"
FT /id="PRO_1000060137"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT MOD_RES 228
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
SQ SEQUENCE 411 AA; 44600 MW; D95ADEF1CB202F21 CRC64;
MGIRNTLDKL EPHFHQGGKY EKFYALYEAV DTIFYSPPSV TKSTAHVRDG IDLKRIMITV
WLCTFPAMFF GMYNAGLQAN MAIGDGFGAL GGWREAVTMA LAGSHDPGSI WANFVLGATY
FLPIYLVTFA VGGFWEVLFA VKRGHEVNEG FFVTSVLYAL ILPATIPLWQ VALGITFGVV
IGKEIFGGTG KNFLNPALTG RAFLYFAYPA QISGDSVWVA ADGYTGATAL STAAQNGMSA
VQQAYSWWDA FLGFIPGSVG ETSTLAILIG AAVLLITRIA SWRIMLGVFV GMALTAMLFT
AIGSESNPMF GMPWYWHLVL GGFAFGMVFM ATDPVSASMT DPGKLLFGFL IGVMTVLIRV
VNPAFPEGIM LAILFANLFA PMIDHFFVQA NIKRRMKRDA AYSPATNEET A
