ID   NUOB_ECOLI              Reviewed;         220 AA.
AC   P0AFC7; P33598; P78090; P78186; P78187;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
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;
DE   AltName: Full=NUO2;
GN   Name=nuoB; OrderedLocusNames=b2287, JW5875;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / AN387;
RX   MEDLINE=93389724; PubMed=7690854; DOI=10.1006/jmbi.1993.1488;
RA   Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.;
RT   "The gene locus of the proton-translocating NADH: ubiquinone
RT   oxidoreductase in Escherichia coli. Organization of the 14 genes and
RT   relationship between the derived proteins and subunits of
RT   mitochondrial complex I.";
RL   J. Mol. Biol. 233:109-122(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   MEDLINE=97349980; PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA   Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA   Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA   Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA   Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA   Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT   K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT   analysis of its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-12.
RC   STRAIN=K12 / EMG2;
RX   MEDLINE=97443975; PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded
RT   in the genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-6.
RX   PubMed=7607227; DOI=10.1111/j.1432-1033.1995.tb20594.x;
RA   Leif H., Sled V.D., Ohnishi T., Weiss H., Friedrich T.;
RT   "Isolation and characterization of the proton-translocating NADH:
RT   ubiquinone oxidoreductase from Escherichia coli.";
RL   Eur. J. Biochem. 230:538-548(1995).
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       ubiquinone. Couples the redox reaction to proton translocation
CC       (for every two electrons transferred, four hydrogen ions are
CC       translocated across the cytoplasmic membrane), and thus conserves
CC       the redox energy in a proton gradient.
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.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein; Cytoplasmic side.
CC   -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
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DR   EMBL; X68301; CAA48361.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75347.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16121.2; -; Genomic_DNA.
DR   PIR; E65000; E65000.
DR   RefSeq; AP_002885.1; -.
DR   RefSeq; NP_416790.1; -.
DR   IntAct; P0AFC7; 1.
DR   TCDB; 3.D.1.1.1; proton-translocating NADH dehydrogenase (NDH) family.
DR   SWISS-2DPAGE; P0AFC7; -.
DR   GeneID; 946738; -.
DR   GenomeReviews; AP009048_GR; JW5875.
DR   GenomeReviews; U00096_GR; b2287.
DR   KEGG; ecj:JW5875; -.
DR   KEGG; eco:b2287; -.
DR   EchoBASE; EB2008; -.
DR   EcoGene; EG12083; nuoB.
DR   HOGENOM; P0AFC7; -.
DR   OMA; P0AFC7; IAGTPFI.
DR   BioCyc; EcoCyc:NUOB-MON; -.
DR   BioCyc; MetaCyc:NUOB-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   1: Evidence at protein level;
KW   4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   NAD; Oxidoreductase; Quinone; Transport; Ubiquinone.
FT   CHAIN         1    220       NADH-quinone oxidoreductase subunit B.
FT                                /FTId=PRO_0000118765.
FT   METAL        63     63       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL        64     64       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       129    129       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       158    158       Iron-sulfur (4Fe-4S) (Potential).
FT   CONFLICT     71     71       S -> L (in Ref. 1; CAA48361).
SQ   SEQUENCE   220 AA;  25056 MW;  EBD6268505993880 CRC64;
     MDYTLTRIDP NGENDRYPLQ KQEIVTDPLE QEVNKNVFMG KLNDMVNWGR KNSIWPYNFG
     LSCCYVEMVT SFTAVHDVAR FGAEVLRASP RQADLMVVAG TCFTKMAPVI QRLYDQMLEP
     KWVISMGACA NSGGMYDIYS VVQGVDKFIP VDVYIPGCPP RPEAYMQALM LLQESIGKER
     RPLSWVVGDQ GVYRANMQSE RERKRGERIA VTNLRTPDEI
//