NUOL_ECOLI
ID NUOL_ECOLI Reviewed; 613 AA.
AC P33607; P78254;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=NADH-quinone oxidoreductase subunit L;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit L;
DE AltName: Full=NDH-1 subunit L;
DE AltName: Full=NUO12;
GN Name=nuoL; OrderedLocusNames=b2278, JW2273;
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 5 family. {ECO:0000305}.
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DR EMBL; X68301; CAA48371.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75338.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16106.1; -; Genomic_DNA.
DR PIR; D64999; D64999.
DR RefSeq; NP_416781.1; NC_000913.3.
DR RefSeq; WP_001056643.1; NZ_LN832404.1.
DR PDB; 7NYH; EM; 3.60 A; L=1-613.
DR PDBsum; 7NYH; -.
DR AlphaFoldDB; P33607; -.
DR SMR; P33607; -.
DR BioGRID; 4260888; 94.
DR ComplexPortal; CPX-243; Respiratory chain complex I.
DR DIP; DIP-10388N; -.
DR IntAct; P33607; 1.
DR STRING; 511145.b2278; -.
DR TCDB; 3.D.1.1.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR jPOST; P33607; -.
DR PaxDb; P33607; -.
DR PRIDE; P33607; -.
DR EnsemblBacteria; AAC75338; AAC75338; b2278.
DR EnsemblBacteria; BAA16106; BAA16106; BAA16106.
DR GeneID; 945540; -.
DR KEGG; ecj:JW2273; -.
DR KEGG; eco:b2278; -.
DR PATRIC; fig|1411691.4.peg.4458; -.
DR EchoBASE; EB2016; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_6_2_6; -.
DR InParanoid; P33607; -.
DR OMA; LIGFWQH; -.
DR PhylomeDB; P33607; -.
DR BioCyc; EcoCyc:NUOL-MON; -.
DR BioCyc; MetaCyc:NUOL-MON; -.
DR PRO; PR:P33607; -.
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; IEA:InterPro.
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:0015990; P:electron transport coupled proton transport; IMP:EcoCyc.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal.
DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR PANTHER; PTHR42829; PTHR42829; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR TIGRFAMs; TIGR01974; NDH_I_L; 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..613
FT /note="NADH-quinone oxidoreductase subunit L"
FT /id="PRO_0000118213"
FT TOPO_DOM 1..6
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..74
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..210
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..281
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..338
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..413
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..494
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..613
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 39
FT /note="G -> A (in Ref. 1; CAA48371)"
FT /evidence="ECO:0000305"
FT CONFLICT 47..58
FT /note="FIGVDFFANGEQ -> LSALISSLTASK (in Ref. 1; CAA48371)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="A -> R (in Ref. 1; CAA48371)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="F -> L (in Ref. 1; CAA48371)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 66438 MW; 7B768F6D4F2668A1 CRC64;
MNMLALTIIL PLIGFVLLAF SRGRWSENVS AIVGVGSVGL AALVTAFIGV DFFANGEQTY
SQPLWTWMSV GDFNIGFNLV LDGLSLTMLS VVTGVGFLIH MYASWYMRGE EGYSRFFAYT
NLFIASMVVL VLADNLLLMY LGWEGVGLCS YLLIGFYYTD PKNGAAAMKA FVVTRVGDVF
LAFALFILYN ELGTLNFREM VELAPAHFAD GNNMLMWATL MLLGGAVGKS AQLPLQTWLA
DAMAGPTPVS ALIHAATMVT AGVYLIARTH GLFLMTPEVL HLVGIVGAVT LLLAGFAALV
QTDIKRVLAY STMSQIGYMF LALGVQAWDA AIFHLMTHAF FKALLFLASG SVILACHHEQ
NIFKMGGLRK SIPLVYLCFL VGGAALSALP LVTAGFFSKD EILAGAMANG HINLMVAGLV
GAFMTSLYTF RMIFIVFHGK EQIHAHAVKG VTHSLPLIVL LILSTFVGAL IVPPLQGVLP
QTTELAHGSM LTLEITSGVV AVVGILLAAW LWLGKRTLVT SIANSAPGRL LGTWWYNAWG
FDWLYDKVFV KPFLGIAWLL KRDPLNSMMN IPAVLSRFAG KGLLLSENGY LRWYVASMSI
GAVVVLALLM VLR
