NUOM_ECOLI
ID NUOM_ECOLI Reviewed; 509 AA.
AC P0AFE8; P31978; P78248;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=b2277, JW2272;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / AN387;
RX PubMed=7690854; DOI=10.1006/jmbi.1993.1488;
RA Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.;
RT "The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase
RT in Escherichia coli. Organization of the 14 genes and relationship between
RT the derived proteins and subunits of mitochondrial complex I.";
RL J. Mol. Biol. 233:109-122(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8366049; DOI=10.1128/jb.175.17.5642-5647.1993;
RA Zambrano M.M., Kolter R.G.;
RT "Escherichia coli mutants lacking NADH dehydrogenase I have a competitive
RT disadvantage in stationary phase.";
RL J. Bacteriol. 175:5642-5647(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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.
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.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the complex I subunit 4 family. {ECO:0000305}.
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DR EMBL; X68301; CAA48372.1; -; Genomic_DNA.
DR EMBL; L19568; AAA53583.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75337.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16105.1; -; Genomic_DNA.
DR PIR; C64999; C64999.
DR RefSeq; NP_416780.1; NC_000913.3.
DR RefSeq; WP_000926441.1; NZ_STEB01000008.1.
DR PDB; 7NYH; EM; 3.60 A; M=1-509.
DR PDB; 7NYR; EM; 3.30 A; M=1-509.
DR PDB; 7NYU; EM; 3.80 A; M=1-509.
DR PDB; 7NYV; EM; 3.70 A; M=1-509.
DR PDBsum; 7NYH; -.
DR PDBsum; 7NYR; -.
DR PDBsum; 7NYU; -.
DR PDBsum; 7NYV; -.
DR AlphaFoldDB; P0AFE8; -.
DR SMR; P0AFE8; -.
DR BioGRID; 4260887; 53.
DR ComplexPortal; CPX-243; Respiratory chain complex I.
DR DIP; DIP-59255N; -.
DR IntAct; P0AFE8; 1.
DR STRING; 511145.b2277; -.
DR TCDB; 3.D.1.1.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR jPOST; P0AFE8; -.
DR PaxDb; P0AFE8; -.
DR PRIDE; P0AFE8; -.
DR DNASU; 947731; -.
DR EnsemblBacteria; AAC75337; AAC75337; b2277.
DR EnsemblBacteria; BAA16105; BAA16105; BAA16105.
DR GeneID; 66673840; -.
DR GeneID; 947731; -.
DR KEGG; ecj:JW2272; -.
DR KEGG; eco:b2277; -.
DR PATRIC; fig|511145.12.peg.2370; -.
DR EchoBASE; EB1722; -.
DR eggNOG; COG1008; Bacteria.
DR HOGENOM; CLU_007100_4_4_6; -.
DR InParanoid; P0AFE8; -.
DR OMA; ITRWGNQ; -.
DR PhylomeDB; P0AFE8; -.
DR BioCyc; EcoCyc:NUOM-MON; -.
DR BioCyc; MetaCyc:NUOM-MON; -.
DR PRO; PR:P0AFE8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0030964; C:NADH dehydrogenase complex; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IDA:EcoCyc.
DR GO; GO:0045271; C:respiratory chain complex I; IC:ComplexPortal.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048039; F:ubiquinone binding; IDA:EcoCyc.
DR GO; GO:0009060; P:aerobic respiration; IMP:EcoCyc.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015990; P:electron transport coupled proton transport; IMP:EcoCyc.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000118039"
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"
FT CONFLICT 464..465
FT /note="EL -> DV (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 2..19
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 27..49
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 85..104
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 114..131
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 170..199
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 231..236
FT /evidence="ECO:0007829|PDB:7NYR"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 265..273
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 274..278
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 280..306
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 312..330
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 335..366
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:7NYR"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 402..417
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 419..425
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 428..443
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 462..480
FT /evidence="ECO:0007829|PDB:7NYR"
FT HELIX 483..502
FT /evidence="ECO:0007829|PDB:7NYR"
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
