ID   NUOB_RICBR              Reviewed;         174 AA.
AC   Q1RJI6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=RBE_0397;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae
RT   in gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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 14 different subunits. Subunits
CC       nuoB, C, D, E, F, and G constitute the peripheral sector of the
CC       complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
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DR   EMBL; CP000087; ABE04478.1; -; Genomic_DNA.
DR   RefSeq; YP_537567.1; -.
DR   GeneID; 3996175; -.
DR   GenomeReviews; CP000087_GR; RBE_0397.
DR   KEGG; rbe:RBE_0397; -.
DR   HOGENOM; Q1RJI6; -.
DR   OMA; Q1RJI6; LINWART.
DR   BioCyc; RBEL336407:RBE_0397-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 inner membrane; Cell membrane; Complete proteome; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; NAD; Oxidoreductase; Quinone;
KW   Transport; Ubiquinone.
FT   CHAIN         1    174       NADH-quinone oxidoreductase subunit B.
FT                                /FTId=PRO_0000287851.
FT   METAL        47     47       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL        48     48       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       112    112       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       142    142       Iron-sulfur (4Fe-4S) (Potential).
SQ   SEQUENCE   174 AA;  19633 MW;  39344EC7DB08A952 CRC64;
     MHNNFYQEDE LLNNELSNRG VLLTKVDDVI GWARSNSLWP MTFGLACCAV EMMQAAASRY
     DMDRFGMLFR PSPRQSDLMI VAGTLTNKMA PALRKVYDQM AEPKWVLSMG SCANGGGYYH
     FSYSVVRGCD RIVPVDVYVP GCPPTAEALI YGLMQLQKKI KRTTGFKYDA RKNH
//