NUOJ_ECOLI
ID NUOJ_ECOLI Reviewed; 184 AA.
AC P0AFE0; P33605; P78236;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=NADH-quinone oxidoreductase subunit J;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit J;
DE AltName: Full=NDH-1 subunit J;
DE AltName: Full=NUO10;
GN Name=nuoJ; OrderedLocusNames=b2280, JW2275;
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].
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 TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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 believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC 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 -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoA, H, J, K, L,
CC M, N constitute the membrane sector of the complex.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the complex I subunit 6 family. {ECO:0000305}.
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DR EMBL; X68301; CAA48369.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75340.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16108.1; -; Genomic_DNA.
DR PIR; F64999; F64999.
DR RefSeq; NP_416783.1; NC_000913.3.
DR RefSeq; WP_000393511.1; NZ_STEB01000008.1.
DR PDB; 7NYH; EM; 3.60 A; J=1-184.
DR PDB; 7NYR; EM; 3.30 A; J=1-184.
DR PDB; 7NYU; EM; 3.80 A; J=1-184.
DR PDB; 7NYV; EM; 3.70 A; J=1-184.
DR PDBsum; 7NYH; -.
DR PDBsum; 7NYR; -.
DR PDBsum; 7NYU; -.
DR PDBsum; 7NYV; -.
DR AlphaFoldDB; P0AFE0; -.
DR SMR; P0AFE0; -.
DR BioGRID; 4260509; 43.
DR ComplexPortal; CPX-243; Respiratory chain complex I.
DR DIP; DIP-59258N; -.
DR IntAct; P0AFE0; 1.
DR STRING; 511145.b2280; -.
DR TCDB; 3.D.1.1.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR jPOST; P0AFE0; -.
DR PaxDb; P0AFE0; -.
DR PRIDE; P0AFE0; -.
DR EnsemblBacteria; AAC75340; AAC75340; b2280.
DR EnsemblBacteria; BAA16108; BAA16108; BAA16108.
DR GeneID; 66673837; -.
DR GeneID; 946756; -.
DR KEGG; ecj:JW2275; -.
DR KEGG; eco:b2280; -.
DR PATRIC; fig|1411691.4.peg.4456; -.
DR EchoBASE; EB2014; -.
DR eggNOG; COG0839; Bacteria.
DR HOGENOM; CLU_085957_0_1_6; -.
DR InParanoid; P0AFE0; -.
DR OMA; WVLPFEA; -.
DR PhylomeDB; P0AFE0; -.
DR BioCyc; EcoCyc:NUOJ-MON; -.
DR BioCyc; MetaCyc:NUOJ-MON; -.
DR PRO; PR:P0AFE0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
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:EcoCyc.
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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:EcoCyc.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal.
DR Gene3D; 1.20.120.1200; -; 1.
DR InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR Pfam; PF00499; Oxidored_q3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Ubiquinone.
FT CHAIN 1..184
FT /note="NADH-quinone oxidoreductase subunit J"
FT /id="PRO_0000118370"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..53
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..137
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 85
FT /note="R -> T (in Ref. 1; CAA48369)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="A -> R (in Ref. 1; CAA48369)"
FT /evidence="ECO:0000305"
FT HELIX 2..19
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 25..46
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 90..111
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 126..132
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 133..137
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 138..158
FT /evidence="ECO:0007829|PDB:7NYR"
SQ SEQUENCE 184 AA; 19875 MW; 9C9D0C9ABAEC7755 CRC64;
MEFAFYICGL IAILATLRVI THTNPVHALL YLIISLLAIS GVFFSLGAYF AGALEIIVYA
GAIMVLFVFV VMMLNLGGSE IEQERQWLKP QVWIGPAILS AIMLVVIVYA ILGVNDQGID
GTPISAKAVG ITLFGPYVLA VELASMLLLA GLVVAFHVGR EERAGEVLSN RKDDSAKRKT
EEHA
