ID   NQRC_VIBPA              Reviewed;         261 AA.
AC   Q87MA8;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=VP2349;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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; BA000031; BAC60612.1; -; Genomic_DNA.
DR   RefSeq; NP_798728.1; NC_004603.1.
DR   RefSeq; WP_005456526.1; NC_004603.1.
DR   AlphaFoldDB; Q87MA8; -.
DR   SMR; Q87MA8; -.
DR   STRING; 223926.28807347; -.
DR   EnsemblBacteria; BAC60612; BAC60612; BAC60612.
DR   GeneID; 1189862; -.
DR   KEGG; vpa:VP2349; -.
DR   PATRIC; fig|223926.6.peg.2252; -.
DR   eggNOG; COG2869; Bacteria.
DR   HOGENOM; CLU_077882_0_1_6; -.
DR   OMA; GLWDAIW; -.
DR   Proteomes; UP000002493; Chromosome 1.
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..261
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   C"
FT                   /id="PRO_0000214225"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
FT   MOD_RES         229
FT                   /note="FMN phosphoryl threonine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
SQ   SEQUENCE   261 AA;  27690 MW;  F9EB20FBA8209A6F CRC64;
     MASNNDSIKK TLGVVIGLSL VCSIIVSTAA VGLRDKQKAN AVLDKQSKIV EVAGIEANGK
     KVPELYAEYI EPRLVDFATG EFVEEAADGS KAANYDQRKA AKDNATSIKL TAEQDKAKII
     RRANTGIVYL VKNGDDVSKV IIPVHGNGLW SMMYAFVAVE TDGNTVSGIT YYEQGETPGL
     GGEVENPSWR AQWVGKKLFD ENHKPAIKVV KGGAPAGSEH GVDGLSGATL TGNGVQGTFD
     FWLGDMGFGP FLAKVRDGGL N