ID   NUOC_JANMA              Reviewed;         198 AA.
AC   A6SY07;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=NADH-quinone oxidoreductase subunit C {ECO:0000255|HAMAP-Rule:MF_01357};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01357};
DE   AltName: Full=NADH dehydrogenase I subunit C {ECO:0000255|HAMAP-Rule:MF_01357};
DE   AltName: Full=NDH-1 subunit C {ECO:0000255|HAMAP-Rule:MF_01357};
GN   Name=nuoC {ECO:0000255|HAMAP-Rule:MF_01357}; OrderedLocusNames=mma_1464;
OS   Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=375286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marseille;
RX   PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA   Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA   Drancourt M.;
RT   "Genome analysis of Minibacterium massiliensis highlights the convergent
RT   evolution of water-living bacteria.";
RL   PLoS Genet. 3:1454-1463(2007).
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. {ECO:0000255|HAMAP-Rule:MF_01357}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01357};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC       D, E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01357}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01357}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01357}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01357}.
CC   -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01357}.
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DR   EMBL; CP000269; ABR89190.1; -; Genomic_DNA.
DR   RefSeq; WP_012079320.1; NC_009659.1.
DR   AlphaFoldDB; A6SY07; -.
DR   SMR; A6SY07; -.
DR   STRING; 375286.mma_1464; -.
DR   EnsemblBacteria; ABR89190; ABR89190; mma_1464.
DR   KEGG; mms:mma_1464; -.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_042628_2_1_4; -.
DR   OMA; MERETYD; -.
DR   OrthoDB; 1735902at2; -.
DR   BioCyc; JSP375286:MMA_RS07620-MON; -.
DR   Proteomes; UP000006388; Chromosome.
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   Gene3D; 3.30.460.80; -; 1.
DR   HAMAP; MF_01357; NDH1_NuoC; 1.
DR   InterPro; IPR010218; NADH_DH_suC.
DR   InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR   InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR   InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   SUPFAM; SSF143243; SSF143243; 1.
DR   TIGRFAMs; TIGR01961; NuoC_fam; 1.
DR   PROSITE; PS00542; COMPLEX1_30K; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW   Reference proteome; Translocase; Transport; Ubiquinone.
FT   CHAIN           1..198
FT                   /note="NADH-quinone oxidoreductase subunit C"
FT                   /id="PRO_0000358114"
SQ   SEQUENCE   198 AA;  22956 MW;  DC16187711746B19 CRC64;
     MTIKLELLEA ALRNALGDQL QSLTQALGEV TIVVKSHDYA SAMRVLRDHA DLRFEEMIDL
     CGVDYSTYGD GLWEGPRFAV VSHLLSIKHN WRVRVRVFAA DDEMPVVASM IDIWATANWY
     EREAFDFFGI LFEGHNDLRR ILTDYGFIGH PFRKDFPVSG YVEMRYDPEQ KRVIYQPVTI
     DPRENVPRVI REEQYGAK