NUOK_ECOLI
ID NUOK_ECOLI Reviewed; 100 AA.
AC P0AFE4; P33606; P76487; P78182;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=NADH-quinone oxidoreductase subunit K {ECO:0000255|HAMAP-Rule:MF_01456};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01456};
DE AltName: Full=NADH dehydrogenase I subunit K {ECO:0000255|HAMAP-Rule:MF_01456};
DE AltName: Full=NDH-1 subunit K {ECO:0000255|HAMAP-Rule:MF_01456};
DE AltName: Full=NUO11;
GN Name=nuoK {ECO:0000255|HAMAP-Rule:MF_01456};
GN OrderedLocusNames=b2279, JW2274;
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 MUTAGENESIS OF 25-ARG-ARG-26; GLU-36 AND GLU-72.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=15996109; DOI=10.1021/bi050708w;
RA Kao M.-C., Nakamaru-Ogiso E., Matsuno-Yagi A., Yagi T.;
RT "Characterization of the membrane domain subunit NuoK (ND4L) of the NADH-
RT quinone oxidoreductase from Escherichia coli.";
RL Biochemistry 44:9545-9554(2005).
RN [6]
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 -!- FUNCTION: There are 2 NADH dehydrogenases in E.coli, however only this
CC complex is able to use dNADH (reduced nicotinamide hypoxanthine
CC dinucleotide, deamino-NADH) and dNADH-DB (dimethoxy-5-methyl-6-decyl-
CC 1,4-benzoquinone) as substrates.
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_01456};
CC -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoA, H,
CC J, K, L, 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 4L family.
CC {ECO:0000255|HAMAP-Rule:MF_01456}.
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DR EMBL; X68301; CAA48370.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75339.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16107.2; -; Genomic_DNA.
DR PIR; E64999; E64999.
DR PIR; S38320; S37068.
DR RefSeq; NP_416782.1; NC_000913.3.
DR RefSeq; WP_000612644.1; NZ_STEB01000008.1.
DR PDB; 7NYH; EM; 3.60 A; K=1-100.
DR PDB; 7NYR; EM; 3.30 A; K=1-100.
DR PDB; 7NYU; EM; 3.80 A; K=1-100.
DR PDB; 7NYV; EM; 3.70 A; K=1-100.
DR PDBsum; 7NYH; -.
DR PDBsum; 7NYR; -.
DR PDBsum; 7NYU; -.
DR PDBsum; 7NYV; -.
DR AlphaFoldDB; P0AFE4; -.
DR SMR; P0AFE4; -.
DR BioGRID; 4260508; 69.
DR ComplexPortal; CPX-243; Respiratory chain complex I.
DR DIP; DIP-51165N; -.
DR IntAct; P0AFE4; 2.
DR STRING; 511145.b2279; -.
DR TCDB; 3.D.1.1.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR jPOST; P0AFE4; -.
DR PaxDb; P0AFE4; -.
DR PRIDE; P0AFE4; -.
DR EnsemblBacteria; AAC75339; AAC75339; b2279.
DR EnsemblBacteria; BAA16107; BAA16107; BAA16107.
DR GeneID; 67516046; -.
DR GeneID; 947580; -.
DR KEGG; ecj:JW2274; -.
DR KEGG; eco:b2279; -.
DR PATRIC; fig|1411691.4.peg.4457; -.
DR EchoBASE; EB2015; -.
DR eggNOG; COG0713; Bacteria.
DR HOGENOM; CLU_144724_0_1_6; -.
DR InParanoid; P0AFE4; -.
DR OMA; NFVAFSY; -.
DR PhylomeDB; P0AFE4; -.
DR BioCyc; EcoCyc:NUOK-MON; -.
DR BioCyc; MetaCyc:NUOK-MON; -.
DR PRO; PR:P0AFE4; -.
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:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal.
DR HAMAP; MF_01456; NDH1_NuoK; 1.
DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K.
DR InterPro; IPR039428; NUOK/Mnh_C1-like.
DR PANTHER; PTHR11434; PTHR11434; 1.
DR Pfam; PF00420; Oxidored_q2; 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 Transport; Ubiquinone.
FT CHAIN 1..100
FT /note="NADH-quinone oxidoreductase subunit K"
FT /id="PRO_0000118524"
FT TOPO_DOM 1..3
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TOPO_DOM 25..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TOPO_DOM 49..59
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01456"
FT TOPO_DOM 81..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 25..26
FT /note="RR->AA: Retains 14% dNADH oxidase and dNADH-DB
FT reductase activity."
FT /evidence="ECO:0000269|PubMed:15996109"
FT MUTAGEN 36
FT /note="E->A: Retains 2% dNADH oxidase and dNADH-DB
FT reductase activity."
FT /evidence="ECO:0000269|PubMed:15996109"
FT MUTAGEN 36
FT /note="E->Q: Retains 2% dNADH oxidase and dNADH-DB
FT reductase activity, neither a membrane potential nor a
FT proton gradient can be formed by isolated membranes."
FT /evidence="ECO:0000269|PubMed:15996109"
FT MUTAGEN 72
FT /note="E->A: Retains 43% dNADH oxidase and dNADH-DB
FT reductase activity."
FT /evidence="ECO:0000269|PubMed:15996109"
FT MUTAGEN 72
FT /note="E->Q: Retains 22% dNADH oxidase and dNADH-DB
FT reductase activity."
FT /evidence="ECO:0000269|PubMed:15996109"
FT CONFLICT 40..41
FT /note="NA -> RP (in Ref. 1; CAA48370)"
FT /evidence="ECO:0000305"
FT CONFLICT 46..59
FT /note="FVVAGSYWGQTDGQ -> LRGRRKLLGPRPTVK (in Ref. 1;
FT CAA48370)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="S -> T (in Ref. 1; CAA48370)"
FT /evidence="ECO:0000305"
FT HELIX 4..24
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 28..52
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 59..86
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:7NYR"
SQ SEQUENCE 100 AA; 10845 MW; CC5AF3946A879383 CRC64;
MIPLQHGLIL AAILFVLGLT GLVIRRNLLF MLIGLEIMIN ASALAFVVAG SYWGQTDGQV
MYILAISLAA AEASIGLALL LQLHRRRQNL NIDSVSEMRG
