NUOB_ECOLI
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 03-AUG-2022, entry version 122.
DE RecName: Full=NADH-quinone oxidoreductase subunit B {ECO:0000255|HAMAP-Rule:MF_01356};
DE EC=7.1.1.- {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};
DE AltName: Full=NUO2;
GN Name=nuoB {ECO:0000255|HAMAP-Rule:MF_01356};
GN OrderedLocusNames=b2287, JW5875;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / AN387;
RX 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 oxidoreductase
RT in Escherichia coli. Organization of the 14 genes and relationship between
RT the derived proteins and subunits of 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 PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT 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 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., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX 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 in the
RT 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-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is ubiquinone. Couples
CC the redox reaction to proton translocation (for every two electrons
CC transferred, four hydrogen ions are translocated across the cytoplasmic
CC membrane), and thus conserves the redox energy in a proton gradient.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC Evidence={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 13 different subunits. Subunits NuoB, CD,
CC E, F, and G constitute the peripheral sector of the complex.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein;
CC Cytoplasmic side.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01356}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; NP_416790.1; NC_000913.3.
DR RefSeq; WP_000386733.1; NZ_STEB01000008.1.
DR RefSeq; WP_046608242.1; NZ_LN832404.1.
DR PDB; 7AWT; EM; 2.73 A; B=1-220.
DR PDB; 7NYR; EM; 3.30 A; B=1-220.
DR PDB; 7NYU; EM; 3.80 A; B=1-220.
DR PDB; 7NYV; EM; 3.70 A; B=1-220.
DR PDB; 7NZ1; EM; 2.10 A; B=1-220.
DR PDBsum; 7AWT; -.
DR PDBsum; 7NYR; -.
DR PDBsum; 7NYU; -.
DR PDBsum; 7NYV; -.
DR PDBsum; 7NZ1; -.
DR AlphaFoldDB; P0AFC7; -.
DR SMR; P0AFC7; -.
DR BioGRID; 4262975; 59.
DR ComplexPortal; CPX-243; Respiratory chain complex I.
DR IntAct; P0AFC7; 1.
DR STRING; 511145.b2287; -.
DR TCDB; 3.D.1.1.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR SWISS-2DPAGE; P0AFC7; -.
DR jPOST; P0AFC7; -.
DR PaxDb; P0AFC7; -.
DR PRIDE; P0AFC7; -.
DR EnsemblBacteria; AAC75347; AAC75347; b2287.
DR EnsemblBacteria; BAA16121; BAA16121; BAA16121.
DR GeneID; 67416717; -.
DR GeneID; 946738; -.
DR KEGG; ecj:JW5875; -.
DR KEGG; eco:b2287; -.
DR PATRIC; fig|1411691.4.peg.4449; -.
DR EchoBASE; EB2008; -.
DR eggNOG; COG0377; Bacteria.
DR HOGENOM; CLU_055737_7_3_6; -.
DR InParanoid; P0AFC7; -.
DR OMA; GPYWEHG; -.
DR PhylomeDB; P0AFC7; -.
DR BioCyc; EcoCyc:NUOB-MON; -.
DR BioCyc; MetaCyc:NUOB-MON; -.
DR PRO; PR:P0AFC7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0030964; C:NADH dehydrogenase complex; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IDA:EcoCyc.
DR GO; GO:0045271; C:respiratory chain complex I; IC:ComplexPortal.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IMP:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:EcoCyc.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IMP:EcoCyc.
DR GO; GO:0015990; P:electron transport coupled proton transport; IMP:EcoCyc.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding; NAD;
KW Quinone; Reference proteome; Translocase; Transport; Ubiquinone.
FT CHAIN 1..220
FT /note="NADH-quinone oxidoreductase subunit B"
FT /id="PRO_0000118765"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT BINDING 158
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01356"
FT CONFLICT 71
FT /note="S -> L (in Ref. 1; CAA48361)"
FT /evidence="ECO:0000305"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 162..176
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 193..197
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:7NZ1"
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
