ID   NUOM_RICTY              Reviewed;         494 AA.
AC   Q68VV6;
DT   06-FEB-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 M;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit M;
DE   AltName: Full=NDH-1 subunit M;
GN   Name=nuoM; OrderedLocusNames=RT0780;
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 {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR   EMBL; AE017197; AAU04236.1; -; Genomic_DNA.
DR   RefSeq; WP_011191211.1; NC_006142.1.
DR   AlphaFoldDB; Q68VV6; -.
DR   SMR; Q68VV6; -.
DR   STRING; 257363.RT0780; -.
DR   EnsemblBacteria; AAU04236; AAU04236; RT0780.
DR   KEGG; rty:RT0780; -.
DR   eggNOG; COG1008; Bacteria.
DR   HOGENOM; CLU_007100_4_4_5; -.
DR   OMA; ITRWGNQ; -.
DR   OrthoDB; 535707at2; -.
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   GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR   InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR   InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   PANTHER; PTHR43507; PTHR43507; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01437; NUOXDRDTASE4.
DR   TIGRFAMs; TIGR01972; NDH_I_M; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; NAD; Quinone; Translocase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..494
FT                   /note="NADH-quinone oxidoreductase subunit M"
FT                   /id="PRO_0000274786"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        206..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        459..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   494 AA;  55545 MW;  9EDE999E57B18BEB CRC64;
     MLELPIISIT IFLPLISVLY ILLFINQSKK ANKLNIYVAM VAMLSSVLTF ILTIYILIEF
     DASNHTYQFV ERYTWLDKIG LEFHVGIDGI AIFFVVLTSF LTLICIIGSI FTIKKYIKEY
     LVCFLLMESF CIGAFTAVNL LLFYLFFEAI LVPMYIIIGV WGGDNRIYAA LKFFLYTFFG
     SVFFLLALIY IYSKIHSFDL TYILALTENI PLFAQKILWW TIFIAFAVKI PMIPFHTWLP
     DAHVQAPTSG SVILAGILLK LGSYGFLRVL LPLLPNVSQE FAIYVIYLSV IAIIYSSLVA
     LAQKDIKQMI AYSSIAHMGY VTIGIFSFTE TGISGAIFQM LSHGVVSSSL FLIVGTLYER
     LHTKEIAKYG GVASKMPVLA TFFMITMLSS IGLPSTSGFI GEFLSLLGIY KVNVVAACIA
     ALGIILGAVY MLKLYKEVML GEITNTEIKH FKDLYRYEIL SIAPLILIII YFGLMPNSIL
     NVFHLSVENL LIKF