ID   NQRF_SHEPU              Reviewed;         301 AA.
AC   Q9LCI7;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 112.
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   Shewanella putrefaciens (Pseudomonas putrefaciens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=24;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IAM 1509;
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; AB024728; BAA83765.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9LCI7; -.
DR   SMR; Q9LCI7; -.
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..>301
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   F"
FT                   /id="PRO_0000074503"
FT   DOMAIN          <1..45
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT   DOMAIN          58..196
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT   REGION          199..>301
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         301
SQ   SEQUENCE   301 AA;  33816 MW;  091F4BB5FFCC8821 CRC64;
     GGSCGQCRVK IKSGGGDILP TEMGHITKKE AKEGCRLACQ VAVKTDMELE LDEEIFGVKK
     WQCEVISNDN KATFIKELLL KLPEGEDVHF KAGGYIQIEA PAHVVKYADF DIPEKYRGDW
     DKYGLFDIVS TVNEDVLRAY SMANYPDEKG RIMLNVRIAT PPSANVPAGK MSSYIFNLKA
     GDKVTISGPF GEFFVKETDA EMVFIGGGAG MAPMRSHIFD QLKSKKTKRK MSFWYGARST
     REVFYQADFD ALAAENDNFV WHVALSEPLP EDNWTGYTGF IHNVIYENYL KNHKAPEDCE
     Y