ID   NUOM_BUCBP              Reviewed;         508 AA.
AC   Q89AT5;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=bbp_154;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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 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; AE016826; AAO26888.1; -; Genomic_DNA.
DR   RefSeq; WP_011091289.1; NC_004545.1.
DR   AlphaFoldDB; Q89AT5; -.
DR   SMR; Q89AT5; -.
DR   STRING; 224915.bbp_154; -.
DR   EnsemblBacteria; AAO26888; AAO26888; bbp_154.
DR   GeneID; 56470698; -.
DR   KEGG; bab:bbp_154; -.
DR   eggNOG; COG1008; Bacteria.
DR   HOGENOM; CLU_007100_4_4_6; -.
DR   OMA; ITRWGNQ; -.
DR   OrthoDB; 535707at2; -.
DR   Proteomes; UP000000601; 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; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..508
FT                   /note="NADH-quinone oxidoreductase subunit M"
FT                   /id="PRO_0000118043"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
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        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        470..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   508 AA;  57986 MW;  B1A99C600CC1F5CA CRC64;
     MLLPMLVSIP FFGGFLCLLF NQKNAKISYY LALTSMALVF ILSLILLFNT INVIVSSISN
     SSWSFEYIVP WIEKFGISFH LAVDRLSILM LNLTSILGLV SVFCSWKKVQ KNIGLFYFGL
     LWTLGSIIGI FISVDLFLFF CFWELSVLPT YFLMIMWGYK DNDRKFYYNN IFSANKFFIY
     SQISGLVLLL STLVLVYTHY IYDHILTFDY DVLKHTSMNI VLESCIMLGF FLAFAIKIPI
     VPFHSWLPDF HCYSPVIGVV DISGILLKTS IYALMRFNIP LFPHSTEIFS SIIMFFGIIT
     IFYGAIVSLF QNNIKRFIAY VSISHMGFIL IAIYSINQVA YQGAIIQLIS YSLSTAALFL
     LSGHVFKSIS TFDIDKMGGL WSKLRWIPGF LLIFSIINLG VPGTGNFVGE FMIFMGCFNS
     HLMIVILSIF SLILLALCSL MFVQKICFGP INNRYDFLCD LNVMTICDFL IFVFLLVLIL
     IIGLYPNIII DVSYSPLCSI RNIFSNFI