NQRC_CHLCV
ID NQRC_CHLCV Reviewed; 319 AA.
AC Q823P3;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
DE Short=Na(+)-NQR subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
DE Short=Na(+)-translocating NQR subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
DE EC=7.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00427};
DE AltName: Full=NQR complex subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
DE AltName: Full=NQR-1 subunit C {ECO:0000255|HAMAP-Rule:MF_00427};
GN Name=nqrC {ECO:0000255|HAMAP-Rule:MF_00427}; OrderedLocusNames=CCA_00364;
OS Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS (Chlamydophila caviae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=227941;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX PubMed=12682364; DOI=10.1093/nar/gkg321;
RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA Fraser C.M.;
RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT examining the role of niche-specific genes in the evolution of the
RT Chlamydiaceae.";
RL Nucleic Acids Res. 31:2134-2147(2003).
CC -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to
CC ubiquinol by two successive reactions, coupled with the transport of
CC Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are
CC probably involved in the second step, the conversion of ubisemiquinone
CC to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00427}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n
CC Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-COMP:9565,
CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389,
CC ChEBI:CHEBI:17976, ChEBI:CHEBI:29101, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=7.2.1.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00427};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00427};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00427}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00427}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00427}.
CC -!- SIMILARITY: Belongs to the NqrC family. {ECO:0000255|HAMAP-
CC Rule:MF_00427}.
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DR EMBL; AE015925; AAP05112.1; -; Genomic_DNA.
DR RefSeq; WP_011006329.1; NC_003361.3.
DR AlphaFoldDB; Q823P3; -.
DR SMR; Q823P3; -.
DR STRING; 227941.CCA_00364; -.
DR EnsemblBacteria; AAP05112; AAP05112; CCA_00364.
DR KEGG; cca:CCA_00364; -.
DR eggNOG; COG2869; Bacteria.
DR HOGENOM; CLU_870677_0_0_0; -.
DR OMA; GLWDAIY; -.
DR OrthoDB; 730368at2; -.
DR Proteomes; UP000002193; 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:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00427; NqrC; 1.
DR InterPro; IPR007329; FMN-bd.
DR InterPro; IPR010204; NqrC.
DR PANTHER; PTHR37838; PTHR37838; 1.
DR Pfam; PF04205; FMN_bind; 1.
DR PIRSF; PIRSF009437; NQR-1_subunit_C; 1.
DR SMART; SM00900; FMN_bind; 1.
DR TIGRFAMs; TIGR01938; nqrC; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Flavoprotein; FMN; Ion transport;
KW Membrane; NAD; Phosphoprotein; Sodium; Sodium transport; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..319
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT C"
FT /id="PRO_0000214211"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
FT MOD_RES 283
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
SQ SEQUENCE 319 AA; 35262 MW; 78FE46DBB4733D08 CRC64;
MSSEKPKPHL NKTWYVILFI FALSLFSSVF LSTVYYILAP FEERAAIFDR DQQMLTAAHV
LDFSGKFQIY EEGSWQPAVY DKKSHLLKVA DQHAPVVTSS VLDAYTQGFV RPLLADKLGQ
MFSFEEKNIN VTEFIEKHQN GHFYQQPLLL FYVILANTEQ ARAMSAADVI KNPSVVRAII
IPISGFGLWG PIYGYLAVEN NGDTVLGTAW YQQAETPGLG ANIANPQWQK QFYGKKIFLQ
AAAGNTDFAT TPLGLEVIKG SVQSAFGTTP KALSSIDGIS GATLTCNGVT EAYAQSLAPY
RNLLISFAKL NQRDHNGSK