NQRC_VIBCH
ID NQRC_VIBCH Reviewed; 257 AA.
AC P0C6E0; Q9X4Q5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=VC_2293;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(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}.
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DR EMBL; AE003852; AAF95437.1; -; Genomic_DNA.
DR PIR; E82094; E82094.
DR RefSeq; NP_231924.1; NC_002505.1.
DR RefSeq; WP_000157902.1; NZ_LT906614.1.
DR PDB; 4P6V; X-ray; 3.50 A; C=1-257.
DR PDBsum; 4P6V; -.
DR AlphaFoldDB; P0C6E0; -.
DR SMR; P0C6E0; -.
DR DIP; DIP-61339N; -.
DR IntAct; P0C6E0; 1.
DR STRING; 243277.VC_2293; -.
DR DNASU; 2613215; -.
DR EnsemblBacteria; AAF95437; AAF95437; VC_2293.
DR GeneID; 57740914; -.
DR KEGG; vch:VC_2293; -.
DR PATRIC; fig|243277.26.peg.2187; -.
DR eggNOG; COG2869; Bacteria.
DR HOGENOM; CLU_077882_0_1_6; -.
DR OMA; GLWDAIW; -.
DR BioCyc; MetaCyc:MON-16199; -.
DR BioCyc; VCHO:VC2293-MON; -.
DR BRENDA; 7.2.1.1; 15862.
DR Proteomes; UP000000584; 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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Flavoprotein; FMN;
KW Ion transport; Membrane; NAD; Phosphoprotein; Reference proteome; Sodium;
KW Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..257
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT C"
FT /id="PRO_0000214223"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
FT MOD_RES 225
FT /note="FMN phosphoryl threonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00427"
FT HELIX 9..29
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 33..52
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 116..129
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 132..143
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 145..156
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 159..169
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 241..244
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:4P6V"
SQ SEQUENCE 257 AA; 27619 MW; 007C09F4FEA4C272 CRC64;
MASNNDSIKK TLFVVIALSL VCSIIVSAAA VGLRDKQKEN AALDKQSKIL QVAGIEAKGS
KQIVELFNKS IEPRLVDFNT GDFVEGDAAN YDQRKAAKEA SESIKLTAEQ DKAKIQRRAN
VGVVYLVKDG DKTSKVILPV HGNGLWSMMY AFVAVETDGN TVSGLTYYEQ GETPGLGGEV
ENPAWRAQWV GKKLFDENHK PAIKIVKGGA PQGSEHGVDG LSGATLTSNG VQNTFDFWLG
DMGFGPFLTK VRDGGLN
