NQRB_VIBCH
ID NQRB_VIBCH Reviewed; 415 AA.
AC Q9KPS2; Q9X4Q4;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 133.
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=VC_2294;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10077658; DOI=10.1073/pnas.96.6.3183;
RA Haese C.C., Mekalanos J.J.;
RT "Effects of changes in membrane sodium flux on virulence gene expression in
RT Vibrio cholerae.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3183-3187(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF95438.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF117331; AAD29963.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF95438.1; ALT_INIT; Genomic_DNA.
DR PIR; F82094; F82094.
DR RefSeq; NP_231925.1; NC_002505.1.
DR RefSeq; WP_000523294.1; NZ_LT906614.1.
DR PDB; 4P6V; X-ray; 3.50 A; B=1-415.
DR PDBsum; 4P6V; -.
DR AlphaFoldDB; Q9KPS2; -.
DR SMR; Q9KPS2; -.
DR DIP; DIP-61338N; -.
DR IntAct; Q9KPS2; 1.
DR STRING; 243277.VC_2294; -.
DR DNASU; 2613216; -.
DR EnsemblBacteria; AAF95438; AAF95438; VC_2294.
DR GeneID; 57740915; -.
DR GeneID; 66939858; -.
DR KEGG; vch:VC_2294; -.
DR PATRIC; fig|243277.26.peg.2188; -.
DR eggNOG; COG1805; Bacteria.
DR HOGENOM; CLU_042020_1_1_6; -.
DR OMA; FNPAYPE; -.
DR BioCyc; MetaCyc:MON-16198; -.
DR BRENDA; 7.2.1.1; 15862.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Flavoprotein; FMN;
KW Ion transport; Membrane; NAD; Phosphoprotein; Reference proteome; Sodium;
KW Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..415
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT B"
FT /id="PRO_0000074444"
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 HELIX 54..61
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 65..84
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 122..150
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 237..243
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 272..288
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 295..314
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 336..342
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 354..373
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 383..404
FT /evidence="ECO:0007829|PDB:4P6V"
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
