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NQRF_SHEDO
ID   NQRF_SHEDO              Reviewed;         408 AA.
AC   Q12QK1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=Sden_0987;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) 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; CP000302; ABE54275.1; -; Genomic_DNA.
DR   RefSeq; WP_011495439.1; NC_007954.1.
DR   AlphaFoldDB; Q12QK1; -.
DR   SMR; Q12QK1; -.
DR   STRING; 318161.Sden_0987; -.
DR   EnsemblBacteria; ABE54275; ABE54275; Sden_0987.
DR   KEGG; sdn:Sden_0987; -.
DR   eggNOG; COG2871; Bacteria.
DR   HOGENOM; CLU_003827_7_2_6; -.
DR   OMA; FIKEFVV; -.
DR   OrthoDB; 1834577at2; -.
DR   Proteomes; UP000001982; Chromosome.
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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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   PRINTS; PR00371; FPNCR.
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;
KW   Reference proteome; Sodium; Sodium transport; Translocase; Transmembrane;
KW   Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..408
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   F"
FT                   /id="PRO_1000080594"
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   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"
SQ   SEQUENCE   408 AA;  44969 MW;  59935AC847F8C393 CRC64;
     MLEVYLGVGM FTAIVLVLVL VILFAKSKLV ASGDIIIGIN GDADKAITTG AGGKLLSVLA
     DNGIFVSSAC GGGGSCGQCR VNIKSGGGDI LPTELDHISK GEARGGCRLS CQVNVKSDME
     IELDEEIFGI KKWECDVISN DNKATFIKEL KLQIPDGESV PFRAGGYIQI EAPAHHVKYA
     DFDVPAKYRG DWEHFGFFKL ESKVDEETIR AYSMANYPEE FGIIMLNVRI ATPPPRNLSL
     PCGKMSSYIW SLKAGDKVTI SGPFGEFFAK DTDAEMVFIG GGAGMAPMRS HLFDQLKRLK
     SKRKMSFWYG ARSKREMFYV EDFDGLAAEN ENFQWHVALS DPQAEDEWTG YTGFIHNVLY
     ENYLRDHDAP EDCEFYMCGP PMMNAAVISM LKDLGVEDEN ILLDDFGG
 
 
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