ID   NUOB_BUCAP              Reviewed;         223 AA.
AC   Q8K9Y6;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 42.
DE   RecName: Full=NADH-quinone oxidoreductase subunit B;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I subunit B;
DE   AltName: Full=NDH-1 subunit B;
GN   Name=nuoB; OrderedLocusNames=BUsg_148;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC       sulfur (Fe-S) centers, to quinones in the respiratory chain.
CC       Couples the redox reaction to proton translocation (for every two
CC       electrons transferred, four hydrogen ions are translocated across
CC       the cytoplasmic membrane), and thus conserves the redox energy in
CC       a proton gradient (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
CC   -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits
CC       nuoB, CD, E, F, and G constitute the peripheral sector of the
CC       complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
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DR   EMBL; AE013218; AAM67716.1; -; Genomic_DNA.
DR   RefSeq; NP_660505.1; -.
DR   GeneID; 1005965; -.
DR   GenomeReviews; AE013218_GR; BUsg_148.
DR   KEGG; bas:BUsg148; -.
DR   HOGENOM; Q8K9Y6; -.
DR   OMA; Q8K9Y6; IAGTPFI.
DR   BioCyc; BAPH198804:BUSG148-MON; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:HAMAP.
DR   GO; GO:0019684; P:photosynthesis, light reaction; IEA:HAMAP.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_01356; -; 1.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR006138; NADH_UbQ_OxRdtase_su-20kDa.
DR   InterPro; IPR014406; NiFe_hyd_3_ssu/Q_oxred_NuoB.
DR   PANTHER; PTHR11995:SF2; NADH_DH_20kDa; 1.
DR   PANTHER; PTHR11995; NiFe_hyd_3_ssu/Q_oxred_NuoB; 1.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR   PROSITE; PS01150; COMPLEX1_20K; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Cell membrane; Complete proteome; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; NAD; Oxidoreductase; Quinone; Transport; Ubiquinone.
FT   CHAIN         1    223       NADH-quinone oxidoreductase subunit B.
FT                                /FTId=PRO_0000118770.
FT   METAL        66     66       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL        67     67       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       132    132       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       161    161       Iron-sulfur (4Fe-4S) (Potential).
SQ   SEQUENCE   223 AA;  25497 MW;  9883840771B302BF CRC64;
     MNYTLTRAER KSQRHYPNET TQSTIDPIEG YLKKNILMGK VTKLLHKIVN WGRKNSLWPY
     NFGLSCCYVE MVTAFTSVHD VARFGSEVLR ASPRQADVMV IAGTPFIKMA PVIQRLYDQM
     LEPKWVISMG ACANSGGMYD IYSVVQGVDK FLPVDIYIPG CPPRPEAYIH ALTLLQKTIN
     EERRPLSWVV GEQGIYRKKM LSEKIQNRKK RISVVNLPTS EKI
//