ID   NUOL_BUCAP              Reviewed;         615 AA.
AC   Q8K9X7;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
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;
GN   Name=nuoL; OrderedLocusNames=BUsg_157;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC       reaction to proton translocation (for every two electrons transferred,
CC       four hydrogen ions are translocated across the cytoplasmic membrane),
CC       and thus conserves the redox energy in a proton gradient (By
CC       similarity). {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR   EMBL; AE013218; AAM67725.1; -; Genomic_DNA.
DR   RefSeq; WP_011053692.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9X7; -.
DR   SMR; Q8K9X7; -.
DR   STRING; 198804.BUsg_157; -.
DR   EnsemblBacteria; AAM67725; AAM67725; BUsg_157.
DR   KEGG; bas:BUsg_157; -.
DR   eggNOG; COG1009; Bacteria.
DR   HOGENOM; CLU_007100_6_2_6; -.
DR   OMA; GVGIMSF; -.
DR   OrthoDB; 1274678at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   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   3: Inferred from homology;
KW   Cell membrane; Membrane; NAD; Quinone; Translocase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..615
FT                   /note="NADH-quinone oxidoreductase subunit L"
FT                   /id="PRO_0000118215"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        457..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        491..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        536..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        594..614
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   615 AA;  70512 MW;  8873DB938A4B7FB1 CRC64;
     MNIIFLIILF PLIGFLFLSL IQGTISERNT NIIGISSIFV SLIITFFYIT GFINYSSQIF
     TQKLFSWISI NELDIDCSLI LDGLSLSMLA MILGIGLLIH IFSTWYMKDK EGYSRFFAYT
     NLFIASMSLL VLADNFLFMY LGWEIVSICS YLLIGFYYKT TNNTSCALKA FVFTRISDVF
     LIISMFLIYN KYGTFNFQEI KFLSNFLNVE DCFDLNVLTL CLLLGVMGKS AQLPLHTWLS
     DAMVGPTPVS ALIHAATMVT AGVYLIARTH FLFLLTPKIL YLISLIGIIT IFISSFSALV
     QQDIKRILAY STMSQIGYMF LALGVKAWTA AIVHLIVHAI FKALLFLSSG SLILSCNNEK
     NIFNLSKVSS KCPLLYVSFL VGGASLVSFP LITSGFYSKG NILFSVLKDG YFNLFLIGLF
     CSFLTSIYTF RMIFVIFHRS SVSFVFSNKR LAHNLPLLIL LFFSTMFGYF IIRLPLFYVF
     PMVKSLENGK FLYEIISSFI SFLGIFIAYH IWIKQPFWFF RFLKFKIIKL IHKFLLNGWY
     FDFFYKILFI HPYLFISKIL SYEPFDFFPT FFVAFIKKTN SIVLKSVNGN VKCYISTMFV
     GINLFFILVL CSFLS