ID   NQRF_COLMA              Reviewed;         303 AA.
AC   Q9K3E1;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
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 maris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=77524;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 16033 / CIP 106458 / JCM 10085 / ABE-1;
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; AB024722; BAA83759.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9K3E1; -.
DR   SMR; Q9K3E1; -.
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_0000074493"
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;  34296 MW;  C9C5A8276A7ACBB3 CRC64;
     GGSCGQCRVE VHSGGGDILP TEEGHINKRE AKSGCRLACQ VAVKQDMEIE VEDEIFGVQQ
     WECEVISNDN KATFIKELKL QIPNGESVPF KAGGYIQIEA PAHHVKYSDF EIDEQYRGDW
     KHFGFFDVES KVDTDTLRAY SMANYPEEEG IIMLNVRIAT PPPGRLHLPA GKMSSYIFSL
     KAGDKVTISG PFGEFFAKET DNEMVFIGGG AGMAPMRSHI FDQLKRLHSK RKMSFWYGAR
     SKREMFYEDD YNGLAADNDN FQWHVALSDP QPEDNWDGLT GFIHNVLFEE YLKDHEAPED
     CEY