ID   NUOB2_BURP1             Reviewed;         167 AA.
AC   Q3JNA0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Putative NADH-quinone oxidoreductase subunit B 2;
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01356};
DE   AltName: Full=NADH dehydrogenase I subunit B 2 {ECO:0000255|HAMAP-Rule:MF_01356};
DE   AltName: Full=NDH-1 subunit B 2 {ECO:0000255|HAMAP-Rule:MF_01356};
GN   Name=nuoB2 {ECO:0000255|HAMAP-Rule:MF_01356};
GN   OrderedLocusNames=BURPS1710b_3588;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC       reaction to proton translocation (for every two electrons transferred,
CC       four hydrogen ions are translocated across the cytoplasmic membrane),
CC       and thus conserves the redox energy in a proton gradient (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01356};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC       D, E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01356}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01356}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01356}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01356}.
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01356}.
CC   -!- CAUTION: This protein lacks the conserved Cys in position 39; it is
CC       replaced by Arg. Thus this protein is probably unable to bind the 4Fe-
CC       4S cluster and may be non-functional. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABA50487.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000124; ABA50487.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004527800.1; NC_007434.1.
DR   AlphaFoldDB; Q3JNA0; -.
DR   SMR; Q3JNA0; -.
DR   EnsemblBacteria; ABA50487; ABA50487; BURPS1710b_3588.
DR   KEGG; bpm:BURPS1710b_3588; -.
DR   HOGENOM; CLU_055737_1_2_4; -.
DR   OrthoDB; 1904620at2; -.
DR   Proteomes; UP000002700; Chromosome I.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_01356; NDH1_NuoB; 1.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW   Transport; Ubiquinone.
FT   CHAIN           1..167
FT                   /note="Putative NADH-quinone oxidoreductase subunit B 2"
FT                   /id="PRO_0000358385"
SQ   SEQUENCE   167 AA;  18550 MW;  C47481A0261F8962 CRC64;
     MANHPLTLEK DGFIVTTLDA AMAAAQKNSL WYMTFGLARC AVEMMHAAGA RYDMDRFGMI
     PRASPRQCDL MIVAGTLTNK MAPAMRRVYD QMAEPRYVVS MGSCANGGGY YHYGYSVVRG
     CDRIVPVDVY VPGCPPTAEA LVYDLMQLQR KVAERSTHSR PKLFARP