ID   NQRC_VIBAN              Reviewed;         255 AA.
AC   Q75R62;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 71.
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};
OS   Vibrio anguillarum (Listonella anguillarum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=55601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Fujiwara-Nagata E., Eguchi Y., Utsumi R., Eguchi M.;
RT   "Cloning, sequencing and transcriptional regulation of Na+-dependent
RT   NADH:quinone oxidoreductase gene of Vibrio anguillarum, a fish pathogen.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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; AB159077; BAD14950.1; -; Genomic_DNA.
DR   RefSeq; WP_013856173.1; NZ_VSLF01000002.1.
DR   AlphaFoldDB; Q75R62; -.
DR   SMR; Q75R62; -.
DR   STRING; 55601.VANGNB10_cI2079c; -.
DR   OMA; GLWDAIW; -.
DR   OrthoDB; 730368at2; -.
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..255
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   C"
FT                   /id="PRO_0000214222"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
FT   MOD_RES         223
FT                   /note="FMN phosphoryl threonine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
SQ   SEQUENCE   255 AA;  27251 MW;  367A9F4355760E71 CRC64;
     MASNNDSIKK TLFVVIALSL VCSIIVSTAA VGLRDKQKVN AVLDKQSKIV EVAGINESGS
     VPELFAKYIE PRLIDFKTGN FVDGDATAYD QRKASKDPAQ SIKLTAEQDK AKIIRRANTG
     VVYLVKSGDE ISKVIVPVHG NGLWSMMYAF VAVETDGNTV SGITYYEQGE TPGLGGEVEN
     PSWRAQFVGK KLFDDNHQPA IKVVKGGAPA GSEHGVDGLS GATLTSNGVQ HTFDFWLGDM
     GFGPFLAKVR DGGLN