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Database: UniProt
Entry: B2S544
LinkDB: B2S544
Original site: B2S544 
ID   NUOB_BRUA1              Reviewed;         193 AA.
AC   B2S544;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   26-NOV-2014, entry version 45.
DE   RecName: Full=NADH-quinone oxidoreductase subunit B {ECO:0000255|HAMAP-Rule:MF_01356};
DE            EC=1.6.99.5 {ECO:0000255|HAMAP-Rule:MF_01356};
DE   AltName: Full=NADH dehydrogenase I subunit B {ECO:0000255|HAMAP-Rule:MF_01356};
DE   AltName: Full=NDH-1 subunit B {ECO:0000255|HAMAP-Rule:MF_01356};
GN   Name=nuoB {ECO:0000255|HAMAP-Rule:MF_01356};
GN   OrderedLocusNames=BAbS19_I07670;
OS   Brucella abortus (strain S19).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=430066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S19;
RX   PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA   Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C.,
RA   Martino-Catt S., Bricker B., Yu G., Du L., Sobral B.W.;
RT   "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT   virulent strains yields candidate virulence genes.";
RL   PLoS ONE 3:E2193-E2193(2008).
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). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC       {ECO:0000255|HAMAP-Rule:MF_01356}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01356};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01356};
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. {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-
CC       Rule:MF_01356}.
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01356}.
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DR   EMBL; CP000887; ACD72291.1; -; Genomic_DNA.
DR   RefSeq; YP_001934765.1; NC_010742.1.
DR   ProteinModelPortal; B2S544; -.
DR   STRING; 430066.BAbS19_I07670; -.
DR   EnsemblBacteria; ACD72291; ACD72291; BAbS19_I07670.
DR   GeneID; 6327929; -.
DR   KEGG; bmc:BAbS19_I07670; -.
DR   PATRIC; 17818584; VBIBruAbo38055_2062.
DR   eggNOG; COG0377; -.
DR   HOGENOM; HOG000228249; -.
DR   KO; K00331; -.
DR   OMA; ISWARTG; -.
DR   OrthoDB; EOG62K20C; -.
DR   BioCyc; BABO430066:GHI6-760-MONOMER; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-HAMAP.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-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:0006810; P:transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.700; -; 1.
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   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    193       NADH-quinone oxidoreductase subunit B.
FT                                /FTId=PRO_0000358357.
FT   METAL        72     72       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01356}.
FT   METAL        73     73       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01356}.
FT   METAL       137    137       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01356}.
FT   METAL       167    167       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_01356}.
SQ   SEQUENCE   193 AA;  21036 MW;  F85E7FEDA4E09A25 CRC64;
     MGLTGTNTTL VAPQPKGILD PRTGKTVGSD DAFFNDLNGE LSDKGFIVTS ADALITWART
     GSLMWMTFGL ACCAVEMMHI SMPRYDAERF GIAPRASPRQ SDVMIVAGTL TNKMAPALRK
     VYDQMPEPRY VISMGSCANG GGYYHYSYSV VRGCDRVVPV DIYVPGCPPT AEALLYGILL
     LQKKIRRTGT IER
//
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