NQRF_VIBCH
ID NQRF_VIBCH Reviewed; 408 AA.
AC Q9X4Q8;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit F {ECO:0000255|HAMAP-Rule:MF_00430};
DE Short=Na(+)-NQR subunit F {ECO:0000255|HAMAP-Rule:MF_00430};
DE Short=Na(+)-translocating NQR subunit F {ECO:0000255|HAMAP-Rule:MF_00430};
DE EC=7.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00430};
DE AltName: Full=NQR complex subunit F {ECO:0000255|HAMAP-Rule:MF_00430};
DE AltName: Full=NQR-1 subunit F {ECO:0000255|HAMAP-Rule:MF_00430};
GN Name=nqrF {ECO:0000255|HAMAP-Rule:MF_00430}; OrderedLocusNames=VC_2290;
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 [GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10077658; DOI=10.1073/pnas.96.6.3183;
RA Haese C.C., Mekalanos J.J.;
RT "Effects of changes in membrane sodium flux on virulence gene expression in
RT Vibrio cholerae.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3183-3187(1999).
RN [2]
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. The first step is
CC catalyzed by NqrF, which accepts electrons from NADH and reduces
CC ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway.
CC {ECO:0000255|HAMAP-Rule:MF_00430}.
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_00430};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00430};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|HAMAP-Rule:MF_00430};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00430};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00430}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00430}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00430}.
CC -!- SIMILARITY: Belongs to the NqrF family. {ECO:0000255|HAMAP-
CC Rule:MF_00430}.
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DR EMBL; AF117331; AAD29967.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF95434.1; -; Genomic_DNA.
DR PIR; B82094; B82094.
DR RefSeq; NP_231921.1; NC_002505.1.
DR RefSeq; WP_000103964.1; NZ_LT906614.1.
DR PDB; 4P6V; X-ray; 3.50 A; F=1-408.
DR PDB; 4U9U; X-ray; 1.55 A; A/B=130-408.
DR PDBsum; 4P6V; -.
DR PDBsum; 4U9U; -.
DR AlphaFoldDB; Q9X4Q8; -.
DR SMR; Q9X4Q8; -.
DR DIP; DIP-61342N; -.
DR IntAct; Q9X4Q8; 1.
DR STRING; 243277.VC_2290; -.
DR DNASU; 2613212; -.
DR EnsemblBacteria; AAF95434; AAF95434; VC_2290.
DR GeneID; 57740911; -.
DR KEGG; vch:VC_2290; -.
DR PATRIC; fig|243277.26.peg.2184; -.
DR eggNOG; COG2871; Bacteria.
DR HOGENOM; CLU_003827_7_2_6; -.
DR OMA; FIKEFVV; -.
DR BioCyc; MetaCyc:MON-16202; -.
DR BioCyc; VCHO:VC2290-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:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_00430; NqrF; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR010205; NqrF.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF000044; Cis_Diol_DH_RD; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR TIGRFAMs; TIGR01941; nqrF; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Cell inner membrane; Cell membrane; FAD;
KW Flavoprotein; Ion transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW NAD; Reference proteome; Sodium; Sodium transport; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..408
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT F"
FT /id="PRO_0000074506"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT DOMAIN 33..127
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT DOMAIN 130..270
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT REGION 273..390
FT /note="Catalytic"
FT BINDING 70
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT BINDING 76
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT BINDING 79
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT BINDING 111
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT HELIX 3..26
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 131..144
FT /evidence="ECO:0007829|PDB:4U9U"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4U9U"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:4U9U"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:4U9U"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:4U9U"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:4U9U"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:4U9U"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:4U9U"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 285..297
FT /evidence="ECO:0007829|PDB:4U9U"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:4U9U"
FT STRAND 333..341
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:4U9U"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:4U9U"
FT TURN 363..366
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:4U9U"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 381..393
FT /evidence="ECO:0007829|PDB:4U9U"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:4U9U"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:4U9U"
SQ SEQUENCE 408 AA; 45067 MW; F5665E9623CAAD7B CRC64;
MSTIIFGVVM FTLIILALVL VILFAKSKLV PTGDITISIN GDPEKAIVTQ PGGKLLTALA
GAGVFVSSAC GGGGSCGQCR VKIKSGGGDI LPTELDHISK GEAREGERLA CQVAVKADMD
LELPEEIFGV KKWECTVISN DNKATFIKEL KLAIPDGESV PFRAGGYIQI EAPAHHVKYA
DFDVPEKYRG DWDKFNLFRY ESKVDEPIIR AYSMANYPEE FGIIMLNVRI ATPPPNNPNV
PPGQMSSYIW SLKAGDKCTI SGPFGEFFAK DTDAEMVFIG GGAGMAPMRS HIFDQLKRLK
SKRKMSYWYG ARSKREMFYV EDFDGLAAEN DNFVWHCALS DPQPEDNWTG YTGFIHNVLY
ENYLKDHEAP EDCEYYMCGP PMMNAAVINM LKNLGVEEEN ILLDDFGG
