ID   NQRF_COLPS              Reviewed;         303 AA.
AC   Q9LCJ2;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Na(+)-translocating NADH-quinone reductase subunit F;
DE            Short=Na(+)-NQR subunit F;
DE            Short=Na(+)-translocating NQR subunit F;
DE            EC=7.2.1.1 {ECO:0000250|UniProtKB:Q56584};
DE   AltName: Full=NQR complex subunit F;
DE   AltName: Full=NQR-1 subunit F;
DE   Flags: Fragment;
GN   Name=nqrF; Synonyms=nqr6;
OS   Colwellia psychrerythraea (Vibrio psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=28229;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27364 / DSM 8813 / NRC 1004;
RX   PubMed=10779868; DOI=10.1139/w00-006;
RA   Kato S., Yumoto I.;
RT   "Detection of the Na(+)-translocating NADH-quinone reductase in marine
RT   bacteria using a PCR technique.";
RL   Can. J. Microbiol. 46:325-332(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:0000250|UniProtKB:Q56584}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q56584};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000250|UniProtKB:A5F5Y4};
CC       Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250|UniProtKB:A5F5Y4};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:A5F5Y4};
CC   -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC       NqrF. {ECO:0000250|UniProtKB:Q56584}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the NqrF family. {ECO:0000305}.
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DR   EMBL; AB024723; BAA83760.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9LCJ2; -.
DR   SMR; Q9LCJ2; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
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: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-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.40.50.80; -; 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; PF00175; NAD_binding_1; 1.
DR   SUPFAM; SSF52343; SSF52343; 1.
DR   SUPFAM; SSF54292; SSF54292; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   TIGRFAMs; TIGR01941; nqrF; 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; Transport; Ubiquinone.
FT   CHAIN           <1..>303
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   F"
FT                   /id="PRO_0000074494"
FT   DOMAIN          <1..45
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          58..198
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          201..>303
FT                   /note="Catalytic"
FT   BINDING         4
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         7
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   BINDING         39
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   NON_TER         1
FT   NON_TER         303
SQ   SEQUENCE   303 AA;  34356 MW;  7620650C92E97278 CRC64;
     GGSCGQCRVE VHSGGGDILP TEEGHINKRE AKSGCRLACQ VAVKQDMEIE VEDEIFGVQQ
     WECEVISNDN QATFIKELKL QIPNGESVPF KAGGYIQIEA PAHHVKYKDF DIDEQYKGDW
     NHFGFFDVES KVDEPTLRAY SMANYPEEEG IIMLNVRIAT PPPGRLHLPA GKMSSFIFSL
     KEGDKVTISG PFGEFFAKET DNEMVFIGGG AGMAPMRSHI FDQLKRLQSK RKMSFWYGAR
     SKREMFYEDD YNGLAADNDN FQWHVALSDP QPEDNWEGMT GFIHNVLFEE YLKDHEAPED
     CEY