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NUOC_XANC5
ID   NUOC_XANC5              Reviewed;         250 AA.
AC   Q3BRN1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=XCV2851;
OS   Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=316273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=85-10;
RX   PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA   Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA   Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA   Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA   Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA   Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA   Kaiser O.;
RT   "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT   Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT   genome sequence.";
RL   J. Bacteriol. 187:7254-7266(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. {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; AM039952; CAJ24530.1; -; Genomic_DNA.
DR   RefSeq; WP_011347939.1; NZ_CP017190.1.
DR   AlphaFoldDB; Q3BRN1; -.
DR   SMR; Q3BRN1; -.
DR   STRING; 456327.BJD11_08615; -.
DR   EnsemblBacteria; CAJ24530; CAJ24530; XCV2851.
DR   GeneID; 63991868; -.
DR   KEGG; xcv:XCV2851; -.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_042628_2_1_6; -.
DR   OMA; MERETYD; -.
DR   Proteomes; UP000007069; 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   PROSITE; PS00542; COMPLEX1_30K; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW   Transport; Ubiquinone.
FT   CHAIN           1..250
FT                   /note="NADH-quinone oxidoreductase subunit C"
FT                   /id="PRO_0000358227"
SQ   SEQUENCE   250 AA;  27817 MW;  128D4A7B12A37D6E CRC64;
     MAEQASSFTD RLAARFAGAQ IAVALPRGEV TLEVAAADWH ATCLALRDEL GFEQLSDLCG
     VDYLGYGSDE WDTADVSSQG FSRGVEGKAV GRFAWGEFPS QESSAGAQPQ QLPKQRFAVV
     AQLISYQHNQ RLRVRCYAPD EQVPVVASLT DIWPGVNWFE REAFDLFGIV FDGHPDLRRI
     LTDYGFVGHP FRKDFPLIGN VEVRYDEERK RVVYEPVTSV EPRVGVPRVI RDDARYETAA
     GEVGKSETAK
 
 
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