ID   NQRC_VIBC1              Reviewed;         261 AA.
AC   Q9RFV9; A7N1U4;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 4.
DT   03-AUG-2022, entry version 127.
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};
GN   OrderedLocusNames=VIBHAR_03273;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11 AND 213-222,
RP   AND MASS SPECTROMETRY.
RX   PubMed=10587447; DOI=10.1021/bi991664s;
RA   Zhou W., Bertsova Y.V., Feng B., Tsatsos P., Verkhovskaya M.L.,
RA   Gennis R.B., Bogachev A.V., Barquera B.;
RT   "Sequencing and preliminary characterization of the Na+-translocating
RT   NADH:ubiquinone oxidoreductase from Vibrio harveyi.";
RL   Biochemistry 38:16246-16252(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) 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   -!- MASS SPECTROMETRY: Mass=28120; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10587447};
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; AF165980; AAF15413.1; -; Genomic_DNA.
DR   EMBL; CP000789; ABU72221.1; -; Genomic_DNA.
DR   RefSeq; WP_012128721.1; NC_022269.1.
DR   AlphaFoldDB; Q9RFV9; -.
DR   SMR; Q9RFV9; -.
DR   EnsemblBacteria; ABU72221; ABU72221; VIBHAR_03273.
DR   KEGG; vha:VIBHAR_03273; -.
DR   PATRIC; fig|338187.25.peg.2919; -.
DR   OMA; GLWDAIW; -.
DR   OrthoDB; 730368at2; -.
DR   Proteomes; UP000008152; Chromosome I.
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   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Direct protein sequencing;
KW   Flavoprotein; FMN; Ion transport; Membrane; NAD; Phosphoprotein; Sodium;
KW   Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10587447"
FT   CHAIN           2..261
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   C"
FT                   /id="PRO_0000214224"
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"
FT   CONFLICT        16
FT                   /note="V -> I (in Ref. 1; AAF15413)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   261 AA;  27791 MW;  CE8016D1422C4745 CRC64;
     MASNNDSIKK TLGVVVGLSL VCSIIVSTAA VGLRDQQKAN AVLDKQSKIV EVAGIDAEGK
     KVPELFAEYI EPRLVDFKTG DFVEKAEDGS TAANYDQRKA AKDPAESIKL TADEDKAKIL
     RRANTGIVYL VKNGDDISKV IIPVHGNGLW SMMYAFVAVE TDGNTVSGIT YYEQGETPGL
     GGEVENPVWR AQFVGKKLFD ENHKPAIKIV KGGAPEGSEH GVDGLSGATL TGNGVQGTFD
     FWLGDMGFGP FLAKVRDGGL N