NQRB_NEIMB
ID NQRB_NEIMB Reviewed; 410 AA.
AC Q9K0M4;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 114.
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=NMB0568;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(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}.
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DR EMBL; AE002098; AAF40996.1; -; Genomic_DNA.
DR PIR; C81185; C81185.
DR RefSeq; NP_273612.1; NC_003112.2.
DR RefSeq; WP_002225562.1; NC_003112.2.
DR AlphaFoldDB; Q9K0M4; -.
DR SMR; Q9K0M4; -.
DR STRING; 122586.NMB0568; -.
DR PaxDb; Q9K0M4; -.
DR EnsemblBacteria; AAF40996; AAF40996; NMB0568.
DR KEGG; nme:NMB0568; -.
DR PATRIC; fig|122586.8.peg.727; -.
DR HOGENOM; CLU_042020_1_1_4; -.
DR OMA; FNPAYPE; -.
DR Proteomes; UP000000425; Chromosome.
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 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..410
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT B"
FT /id="PRO_0000074439"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
FT MOD_RES 232
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00426"
SQ SEQUENCE 410 AA; 44601 MW; F632E12206170B4F CRC64;
MGLKHFLEKI EPHFLPGGKH EKWYALYEAA ATIFYTSGAV TRKAAHVRDA LDSKRMMILV
WLALFPAMFY GMYNVGAQAF GALTPDLLQQ NIANDWHYAF ANALGINMSS EAGVSDKMLF
GAIYFLPIYA TVFVVGGFWE VLFATVRKHE INEGFFVTSI LFALIVPPTL PLWQAALGIS
FGVVVAKEVF GGTGKNFMNP ALAGRAFLFF AYPANLSGDA VWTAVDGYSG ATALAQWAAH
GADGLKNAVT GQTITWMDAF IGKLPGSIGE VSTLALLIGG AFIVFARIAS WRIIAGVMIG
MIAMSSLFNF IGSDTNAMFA MPWYWHLVVG GFAIGMLFMA TDPVSASFTN VGKWWYGALI
GVMCVLIRVV NPAYPEGMML AILFANLFAP IFDYFVAQAN IKRRKARSNG
