ID   NUOC_MYCS2              Reviewed;         238 AA.
AC   A0QU34; I7FZB4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 92.
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};
GN   OrderedLocusNames=MSMEG_2061, MSMEI_2016;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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 a
CC       menaquinone. 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 membrane {ECO:0000255|HAMAP-Rule:MF_01357};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01357};
CC       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; CP000480; ABK70554.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP38487.1; -; Genomic_DNA.
DR   RefSeq; WP_011728124.1; NZ_SIJM01000021.1.
DR   RefSeq; YP_886422.1; NC_008596.1.
DR   AlphaFoldDB; A0QU34; -.
DR   SMR; A0QU34; -.
DR   STRING; 246196.MSMEI_2016; -.
DR   EnsemblBacteria; ABK70554; ABK70554; MSMEG_2061.
DR   EnsemblBacteria; AFP38487; AFP38487; MSMEI_2016.
DR   GeneID; 66733489; -.
DR   KEGG; msg:MSMEI_2016; -.
DR   KEGG; msm:MSMEG_2061; -.
DR   PATRIC; fig|246196.19.peg.2037; -.
DR   eggNOG; COG0852; Bacteria.
DR   OMA; RFELCTG; -.
DR   OrthoDB; 1735902at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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   Pfam; PF00329; Complex1_30kDa; 1.
DR   SUPFAM; SSF143243; SSF143243; 1.
DR   TIGRFAMs; TIGR01961; NuoC_fam; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW   Transport.
FT   CHAIN           1..238
FT                   /note="NADH-quinone oxidoreductase subunit C"
FT                   /id="PRO_0000358137"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   238 AA;  26580 MW;  7CB55207014DD1CE CRC64;
     MSTSNGSANG TNGVGLPRGD EPEIIAVRRG MFGNRDTGDT SGYGRLVRPV ALPGSTPRPY
     GGYFDAVMDR LAEVLGEERY AMSIERVVVY RDQLTIEVSR VQLPAVASVL RDDPDLRFEL
     CLGVSGVHYP EDTGRELHAV YPLMSITHNR RIQLEVAAPD ADPHIPSLYA VYPTTDWHER
     ETYDFFGIIF DGHPSLTRIE MPDDWEGHPQ RKDYPLGGIP VEYHGAQIPP PDQRRSYS