ID   NQRB_PSEA7              Reviewed;         403 AA.
AC   A6V398;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=PSPA7_2161;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-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; CP000744; ABR80839.1; -; Genomic_DNA.
DR   RefSeq; WP_012075156.1; NC_009656.1.
DR   AlphaFoldDB; A6V398; -.
DR   SMR; A6V398; -.
DR   EnsemblBacteria; ABR80839; ABR80839; PSPA7_2161.
DR   KEGG; pap:PSPA7_2161; -.
DR   HOGENOM; CLU_042020_1_1_6; -.
DR   OMA; FNPAYPE; -.
DR   OrthoDB; 1654433at2; -.
DR   Proteomes; UP000001582; 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; Sodium; Sodium transport; Translocase;
KW   Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..403
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   B"
FT                   /id="PRO_1000060143"
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        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT   TRANSMEM        348..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT   TRANSMEM        371..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT   MOD_RES         230
FT                   /note="FMN phosphoryl threonine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
SQ   SEQUENCE   403 AA;  44097 MW;  9955CF04B1E7536B CRC64;
     MGLRNLLDKV EHHFEKGGRY EKWYPLYEAV DTFLYRPGSV TRTTAHVRDG IDLKRMMIIV
     WLCTFPAMFF GMYNVGHQAN LIFAQSPDLL GAQDGWRFAL IGALAGFDPN SLWDCLVQGA
     AYFLPVYLTT FIVGGFWEVL FATIRRHEVN EGFFVTSVLF ALTLPPSVPL WQVALGISFG
     VVLGKEVFGG TGKNFLNPAL VGRAFLFFAY PAQMSGDAVW TSVDGFAGAT SLSLAAAGGV
     DNILGHGLTW MDAFLGHMQG SMGETSTLAI FIGGAVLLLT RIASWRIVAG VMLGMIAMSY
     LFNAIGSTSN PMFAMPWYWH LVTGGFAFGM IFMATDPVSA SMTDTGKWLF GALIGVMVML
     IRVVNPAFPE GMMLAILFAN LFAPLIDHFV VQANIKRRLA RNG