ID   NUOM_RICFE              Reviewed;         493 AA.
AC   Q4UK26;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=RF_1258;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000053; AAY62109.1; -; Genomic_DNA.
DR   RefSeq; WP_011271558.1; NC_007109.1.
DR   AlphaFoldDB; Q4UK26; -.
DR   SMR; Q4UK26; -.
DR   STRING; 315456.RF_1258; -.
DR   EnsemblBacteria; AAY62109; AAY62109; RF_1258.
DR   KEGG; rfe:RF_1258; -.
DR   eggNOG; COG1008; Bacteria.
DR   HOGENOM; CLU_007100_4_4_5; -.
DR   OMA; ITRWGNQ; -.
DR   OrthoDB; 535707at2; -.
DR   Proteomes; UP000008548; 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..493
FT                   /note="NADH-quinone oxidoreductase subunit M"
FT                   /id="PRO_0000275926"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        334..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        458..478
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   493 AA;  55251 MW;  CE4766B4B8C74F7D CRC64;
     MLELPIISIS IFLPLISVLY ILLFISQSKK ADKAIYVMYV AVLSSVLTFI STIYILIEFD
     SSNPAYQFIE RYAWLDKIGL EFHVGVDGIS IFFVALTSFL TLICIIGSLF TVKKYIKEYL
     VCFLLMESFC IGAFTSVNLL LFYLFFEAIL VPMYIIIGVW GGENRIYAAL KFFLYTFFGS
     VFFLLSLIYI YSKIHNFDLT YIPELTGNIP LFTQQILWWA IFIAFAVKIP IIPFHTWLPD
     AHVQAPTSGS VILAGILLKF GGYGFLRVLL PLFSSVSQEF AIYVIYLSVI AIIYASLVAL
     AQKDMKKMIA YSSIAHMGYV TIGIFSFTEA GVSGAIFQML SHGVISSCLF LIVGTLYERL
     HTKEIAKYGG VASKMPVLAT FFMIAMLGSV GLPGTSGFIG EFLSLLGIYK VNVIATFIAA
     LGIILGAVYM LKLYKEVMLG EITNKEIMHF RDLYKYEIIS IAPLILLIIY FGLMPSSILN
     VFRLSVESLL VKF