ID   NUOJ_BUCAP              Reviewed;         163 AA.
AC   Q8K9X9;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 100.
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;
GN   Name=nuoJ; OrderedLocusNames=BUsg_155;
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 6 family. {ECO:0000305}.
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DR   EMBL; AE013218; AAM67723.1; -; Genomic_DNA.
DR   RefSeq; WP_011053690.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9X9; -.
DR   SMR; Q8K9X9; -.
DR   STRING; 198804.BUsg_155; -.
DR   EnsemblBacteria; AAM67723; AAM67723; BUsg_155.
DR   KEGG; bas:BUsg_155; -.
DR   eggNOG; COG0839; Bacteria.
DR   HOGENOM; CLU_085957_0_1_6; -.
DR   OMA; WVLPFEA; -.
DR   OrthoDB; 1683794at2; -.
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   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   3: Inferred from homology;
KW   Cell membrane; Membrane; NAD; Quinone; Translocase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..163
FT                   /note="NADH-quinone oxidoreductase subunit J"
FT                   /id="PRO_0000118375"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   163 AA;  18381 MW;  48F06910F4C32E04 CRC64;
     MEFVFYACSL IAVISTLLVI IQKNAVYSLL YLIISLLSIS GIFFIFGAFF AGALEVVIYA
     GAIIVLFVFV IMMLNLGKKN DLQEKKYLNP IFWIGPSFLS LILFLLMTYA IFFVKDKQIY
     FSLIDVKEVG INLFGPYLLL VELSSLLLLS ALVVVFHIGK EKK