ID NUOB_YERPE Reviewed; 225 AA.
AC Q7CJ93; Q74T28;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 01-MAY-2013, entry version 60.
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=YPO2554, y1631, YP_2365;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/JB.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C.,
RA Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V.,
RA Straley S.C., McDonough K.A., Nilles M.L., Matson J.S., Blattner F.R.,
RA Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G.,
RA Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V.,
RA Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M.,
RA Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z.,
RA Jin L., Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J.,
RA Yang H., Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC immediate electron acceptor for the enzyme in this species is
CC believed to be ubiquinone. Couples the redox reaction to proton
CC translocation (for every two electrons transferred, four hydrogen
CC ions are translocated across the cytoplasmic membrane), and thus
CC conserves the redox energy in 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 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; AE009952; AAM85200.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62570.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL21179.1; -; Genomic_DNA.
DR PIR; AH0311; AH0311.
DR RefSeq; NP_668949.1; NC_004088.1.
DR RefSeq; NP_993693.1; NC_005810.1.
DR RefSeq; YP_002347515.1; NC_003143.1.
DR ProteinModelPortal; Q7CJ93; -.
DR STRING; 214092.YPO2554; -.
DR PRIDE; Q7CJ93; -.
DR DNASU; 1146578; -.
DR EnsemblBacteria; AAM85200; AAM85200; y1631.
DR EnsemblBacteria; AAS62570; AAS62570; YP_2365.
DR GeneID; 1146578; -.
DR GeneID; 1175385; -.
DR GeneID; 2766086; -.
DR KEGG; ype:YPO2554; -.
DR KEGG; ypk:y1631; -.
DR KEGG; ypm:YP_2365; -.
DR eggNOG; COG0377; -.
DR HOGENOM; HOG000228249; -.
DR KO; K00331; -.
DR OMA; PRPEAYI; -.
DR ProtClustDB; PRK06411; -.
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:0019684; P:photosynthesis, light reaction; IEA:HAMAP.
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 InterPro; IPR014406; NiFe-hyd_3_ssu/Q_oxred_NuoB.
DR PANTHER; PTHR11995; PTHR11995; 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 Reference proteome; Transport; Ubiquinone.
FT CHAIN 1 225 NADH-quinone oxidoreductase subunit B.
FT /FTId=PRO_0000376410.
FT METAL 68 68 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 69 69 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 134 134 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 163 163 Iron-sulfur (4Fe-4S) (Potential).
SQ SEQUENCE 225 AA; 25611 MW; 41BA61A5DE98BBCC CRC64;
MDYTLTRIDP NGENDRYPLQ TQETVSGDPL EQHVHRSVYM GKLENAMHDM VNWGRKNSLW
PYNFGLSCCY VEMVTSFTAV HDVARFGAEV LRASPRQADF MVVAGTCFTK MAPVIQRLYE
QMLEPKWVIS MGACANSGGM YDIYSVVQGV DKFLPVDVYI PGCPPRPEAY MQALLLLQES
IGKERRPLSW VVGDQGVYRA NMQPERERKH AERIAVTNLR TPDEI
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