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NUOM_ECO57
ID   NUOM_ECO57              Reviewed;         509 AA.
AC   P0AFE9; P31978; P78248;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
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;
DE   AltName: Full=NUO13;
GN   Name=nuoM; OrderedLocusNames=Z3536, ECs3161;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient (By 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 inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG57406.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB36584.1; -; Genomic_DNA.
DR   PIR; A91024; A91024.
DR   PIR; B85868; B85868.
DR   RefSeq; NP_311188.1; NC_002695.1.
DR   RefSeq; WP_000926441.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AFE9; -.
DR   SMR; P0AFE9; -.
DR   STRING; 155864.EDL933_3440; -.
DR   EnsemblBacteria; AAG57406; AAG57406; Z3536.
DR   EnsemblBacteria; BAB36584; BAB36584; ECs_3161.
DR   GeneID; 66673840; -.
DR   GeneID; 916869; -.
DR   KEGG; ece:Z3536; -.
DR   KEGG; ecs:ECs_3161; -.
DR   PATRIC; fig|386585.9.peg.3299; -.
DR   eggNOG; COG1008; Bacteria.
DR   HOGENOM; CLU_007100_4_4_6; -.
DR   OMA; ITRWGNQ; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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 inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Ubiquinone.
FT   CHAIN           1..509
FT                   /note="NADH-quinone oxidoreductase subunit M"
FT                   /id="PRO_0000118040"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        22..29
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        51..82
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..173
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..221
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..258
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        280..285
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        307..313
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        335..339
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        361..382
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        383..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        425
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        426..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        447..464
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        465..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        486..509
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   509 AA;  56525 MW;  3F8395683908EF97 CRC64;
     MLLPWLILIP FIGGFLCWQT ERFGVKVPRW IALITMGLTL ALSLQLWLQG GYSLTQSAGI
     PQWQSEFDMP WIPRFGISIH LAIDGLSLLM VVLTGLLGVL AVLCSWKEIE KYQGFFHLNL
     MWILGGVIGV FLAIDMFLFF FFWEMMLVPM YFLIALWGHK ASDGKTRITA ATKFFIYTQA
     SGLVMLIAIL ALVFVHYNAT GVWTFNYEEL LNTPMSSGVE YLLMLGFFIA FAVKMPVVPL
     HGWLPDAHSQ APTAGSVDLA GILLKTAAYG LLRFSLPLFP NASAEFAPIA MWLGVIGIFY
     GAWMAFAQTD IKRLIAYTSV SHMGFVLIAI YTGSQLAYQG AVIQMIAHGL SAAGLFILCG
     QLYERIHTRD MRMMGGLWSK MKWLPALSLF FAVATLGMPG TGNFVGEFMI LFGSFQVVPV
     ITVISTFGLV FASVYSLAML HRAYFGKAKS QIASQELPGM SLRELFMILL LVVLLVLLGF
     YPQPILDTSH SAIGNIQQWF VNSVTTTRP
 
 
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