ID   NUOJ_RICTY              Reviewed;         205 AA.
AC   Q68VV9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=RT0777;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the complex I subunit 6 family. {ECO:0000305}.
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DR   EMBL; AE017197; AAU04233.1; -; Genomic_DNA.
DR   RefSeq; WP_011191208.1; NC_006142.1.
DR   AlphaFoldDB; Q68VV9; -.
DR   SMR; Q68VV9; -.
DR   STRING; 257363.RT0777; -.
DR   EnsemblBacteria; AAU04233; AAU04233; RT0777.
DR   KEGG; rty:RT0777; -.
DR   eggNOG; COG0839; Bacteria.
DR   HOGENOM; CLU_085957_5_1_5; -.
DR   OMA; MLVNKRE; -.
DR   OrthoDB; 1683794at2; -.
DR   Proteomes; UP000000604; 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..205
FT                   /note="NADH-quinone oxidoreductase subunit J"
FT                   /id="PRO_0000287841"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   205 AA;  23101 MW;  D03E136B793C31AC CRC64;
     MPIFFYLFTT LIIISSLCVV LSKNSVYSVL WLIFTFINAA GLMILLGAEF LAMLLIVIYV
     GAVAVLFLFV IMMLDINFNQ AITKLRENLS LSIFITLIMF VDLVITVILS TKNINHSSNI
     SFAIANNISN TKAIGSVLYT DFMLPFQMAG LILFVAMISC ITLTLKKRER VKYQDIRKQL
     SHNKGNVILM TKPILNKGVE NIKYE