NUOM_RICCN
ID NUOM_RICCN Reviewed; 493 AA.
AC Q92G96;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=RC1227;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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; AE006914; AAL03765.1; -; Genomic_DNA.
DR PIR; C97853; C97853.
DR RefSeq; WP_010977792.1; NC_003103.1.
DR AlphaFoldDB; Q92G96; -.
DR SMR; Q92G96; -.
DR EnsemblBacteria; AAL03765; AAL03765; RC1227.
DR KEGG; rco:RC1227; -.
DR PATRIC; fig|272944.4.peg.1406; -.
DR HOGENOM; CLU_007100_4_4_5; -.
DR OMA; ITRWGNQ; -.
DR Proteomes; UP000000816; 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_0000118046"
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; 55204 MW; 9686939BCC3BE592 CRC64;
MLELPIISIS IFLPLISVLY ILLFISQSKK ADKPIYVMYV AVLSSVLTFI STIYILIEFD
SSNPAYQFVE RYAWLDKIGL EFHVGVDGIS ILFVVLTSFL TLICIIGSLF TVKKYIKEYL
VCFLLMESFC IGAFTSVNLL LFYLFFEAIL VPMYIIIGVW GGKNRIYAAL KFFLYTFFGS
VFFLLSLIYI YSKMHSFDLT YIFQLTDNIP LFAQQILWWA IFIAFAVKIP IIPFHTWLPD
AHVQAPTSGS VILAGILLKL GGYGFLRVLL PLCPSVSQEF AIYVIYLSVI AIIYASLVAL
AQKDMKKMIA YSSIAHMGYV TIGIFSFTKA GVSGAIFQML SHGVISSCLF LIVGTLYERL
HTKEIAKYGG VASKMPVLAA FFMIAMLGSV GLPGTSGFIG EFLSLLGIYK VNVVATFIAA
LGIIFGAVYM LKLYKEVMLG EITNKEIMHF RDLYKYEIIS IAPLILLIIY FGLMPSSILN
VFSLSVENLL VKF