NQRC_NEIMB
ID NQRC_NEIMB Reviewed; 258 AA.
AC Q9K0M5;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 115.
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=NMB0567;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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 -!- CAUTION: The residue potentially involved in the covalent binding of
CC FMN is a Ser instead of a Thr. {ECO:0000255|HAMAP-Rule:MF_00427,
CC ECO:0000305}.
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; AE002098; AAF40995.1; -; Genomic_DNA.
DR PIR; B81185; B81185.
DR RefSeq; NP_273611.1; NC_003112.2.
DR RefSeq; WP_002225563.1; NC_003112.2.
DR AlphaFoldDB; Q9K0M5; -.
DR SMR; Q9K0M5; -.
DR STRING; 122586.NMB0567; -.
DR PaxDb; Q9K0M5; -.
DR EnsemblBacteria; AAF40995; AAF40995; NMB0567.
DR KEGG; nme:NMB0567; -.
DR PATRIC; fig|122586.8.peg.726; -.
DR HOGENOM; CLU_077882_0_1_4; -.
DR OMA; GLWDAIW; -.
DR Proteomes; UP000000425; 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..258
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT C"
FT /id="PRO_0000214218"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
FT MOD_RES 226
FT /note="FMN phosphoryl serine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
SQ SEQUENCE 258 AA; 27607 MW; 1F20D8EF011F7C3E CRC64;
MAKKFDKDSF SGTLIVVLAV SLICSVIVAG AVVGLKPIQE KQKLQDKQGY ILSVAGLMDK
DTDIGKTFAE RIEQRVVDLA TGEYVADAPK DFSARIAGKD PAQSIRIKTE DDLAGIKSRA
KYTEVYLVKG EDGKIGQIIL PMHGNGLWSV MYGFVAIQPD GNTINGITYY EQGETPGLGG
EIGNPLWQQK FVGKKLFDGQ GKLALHVGKG AGSDKEHGVD ALSGASLTSK GVQGSFAYWF
GENGYIPYLN KLKSAGAQ
