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NQRF_VIBVU
ID   NQRF_VIBVU              Reviewed;         407 AA.
AC   Q8DBJ1;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 129.
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=VV1_1826;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) 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. 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; AE016795; AAO10232.1; -; Genomic_DNA.
DR   RefSeq; WP_011079732.1; NC_004459.3.
DR   AlphaFoldDB; Q8DBJ1; -.
DR   SMR; Q8DBJ1; -.
DR   EnsemblBacteria; AAO10232; AAO10232; VV1_1826.
DR   GeneID; 66965759; -.
DR   KEGG; vvu:VV1_1826; -.
DR   HOGENOM; CLU_003827_7_2_6; -.
DR   OMA; FIKEFVV; -.
DR   Proteomes; UP000002275; 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   CDD; cd00207; fer2; 1.
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   3: Inferred from homology;
KW   2Fe-2S; Cell inner membrane; Cell membrane; FAD; Flavoprotein;
KW   Ion transport; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; Sodium;
KW   Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..407
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   F"
FT                   /id="PRO_0000074510"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   DOMAIN          32..126
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   DOMAIN          129..269
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   REGION          272..389
FT                   /note="Catalytic"
FT   BINDING         69
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   BINDING         75
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   BINDING         78
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   BINDING         110
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
SQ   SEQUENCE   407 AA;  44945 MW;  1FDEC95F196715A2 CRC64;
     MDIILGVVMF TLIVLALVLV ILFAKSKLVP TGDITISING DADKSIVTSP GGKLLSALAG
     AGVFVSSACG GGGSCGQCRV KVKSGGGDIL PTELDHITKG EAREGERLAC QVAVKTDMDI
     ELPEEIFGVK KWECTVISND NKATFIKELK LQIPDGESVP FRAGGYIQIE APAHHVKYAD
     FDVPEEYRGD WDKFNLFRYE SIVKEDIIRA YSMANYPEEF GIIMLNVRIA TPPPNNPDVA
     PGQMSSYIWS LKEGDKCTIS GPFGEFFAKD TDAEMVFIGG GAGMAPMRSH IFDQLKRLKS
     KRKMSYWYGA RSKREMFYVE DFDGLAAEND NFVWHCALSD PLPEDNWDGY TGFIHNVLYE
     NYLRDHDAPE DCEYYMCGPP MMNAAVIGML KNLGVEDENI LLDDFGG
 
 
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