NQRC_HAEIN
ID NQRC_HAEIN Reviewed; 244 AA.
AC P43957;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=HI_0167;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION AS NQR SYSTEM.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=8601449; DOI=10.1016/0014-5793(96)00114-7;
RA Hayashi M., Nakayama Y., Unemoto T.;
RT "Existence of Na+-translocating NADH-quinone reductase in Haemophilus
RT influenzae.";
RL FEBS Lett. 381:174-176(1996).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L42023; AAC21838.1; -; Genomic_DNA.
DR PIR; B64003; B64003.
DR RefSeq; NP_438336.1; NC_000907.1.
DR RefSeq; WP_005653794.1; NC_000907.1.
DR AlphaFoldDB; P43957; -.
DR SMR; P43957; -.
DR STRING; 71421.HI_0167; -.
DR EnsemblBacteria; AAC21838; AAC21838; HI_0167.
DR KEGG; hin:HI_0167; -.
DR PATRIC; fig|71421.8.peg.172; -.
DR eggNOG; COG2869; Bacteria.
DR HOGENOM; CLU_077882_0_1_6; -.
DR OMA; GLWDAIW; -.
DR PhylomeDB; P43957; -.
DR BioCyc; HINF71421:G1GJ1-178-MON; -.
DR Proteomes; UP000000579; 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; Reference proteome; Sodium;
KW Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..244
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT C"
FT /id="PRO_0000214216"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
FT MOD_RES 213
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
SQ SEQUENCE 244 AA; 26662 MW; 852560EE2CF1FAC8 CRC64;
MAKFNKDSVG GTILVVLLLS LVCSIIVAGS AVMLKPAQEE QKLLDKQKNI LNVAGLLQEN
TNVKETYAKF IEPRFVDLAT GEYTQQADDS QQAIPADADK ARIRSRSKTT EVYLVKDEQG
QTQQVILPIY GTGLWSVMYG LVSVQPDGNT INGITYYQHG ETPGLGGEIE NPNWASLFKG
KKLFDEQHQP AIRIVKGQAP QDEHSIDGLS GATLTGNGVQ GTFNYWFSKD GFGPYLEKLH
SGAN
