ID   NUOB_RICFE              Reviewed;         174 AA.
AC   Q4UM06;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=RF_0566;
OS   Rickettsia felis (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=42862;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61417.1; -; Genomic_DNA.
DR   RefSeq; YP_246582.1; -.
DR   GeneID; 3400345; -.
DR   GenomeReviews; CP000053_GR; RF_0566.
DR   KEGG; rfe:RF_0566; -.
DR   NMPDR; fig|315456.3.peg.400; -.
DR   HOGENOM; Q4UM06; -.
DR   OMA; Q4UM06; LINWART.
DR   BioCyc; RFEL315456:RF_0566-MON; -.
DR   BRENDA; 1.6.99.5; 297363.
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_0000287852.
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;  19639 MW;  1B89DA83ADCAAA3C CRC64;
     MKHSFYQEDE LLNNELSNRG FLLTKVDDVI GWARANSLWP MTFGLACCAV EMMQAAASRY
     DMDRFGMLFR PSPRQSDLMI VAGTLTNKMA PALRKVYDQM AEPKWVLSMG SCANGGGYYH
     FSYSVVRGCD RIVPVDVYVP GCPPTAEALI YGLMQLQKKI KRTTGFKYDA RQTH
//