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NQRF_PSEAB
ID   NQRF_PSEAB              Reviewed;         407 AA.
AC   Q02PF8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=PA14_25350;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ12233.1; -; Genomic_DNA.
DR   RefSeq; WP_003091181.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02PF8; -.
DR   SMR; Q02PF8; -.
DR   PRIDE; Q02PF8; -.
DR   EnsemblBacteria; ABJ12233; ABJ12233; PA14_25350.
DR   KEGG; pau:PA14_25350; -.
DR   HOGENOM; CLU_003827_7_2_6; -.
DR   OMA; FIKEFVV; -.
DR   Proteomes; UP000000653; 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   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_1000080590"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   DOMAIN          35..127
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   DOMAIN          130..269
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   407 AA;  45501 MW;  21176F6C1C7C3144 CRC64;
     MIGFEIFLAI GMFTAIVLGL VAIILVARAK LVSSGDVTIQ INGEHSLTVP AGGKLLQTLA
     TNNVFLSSAC GGGGTCAQCK CVVVEGGGEM LPTEESHFTR RQAKEGWRLS CQTPVKQDMQ
     IRVPEEVFGV KKWECTVESN PNVATFIKEL TLRLPDGESV DFRAGGYVQL ECPPHVVEYK
     DFDIQPEYRG DWDKFNMWRY VSKVDETVIR AYSMANYPEE QGVVKFNIRI ASPPPGSDLP
     PGQMSSWVFN LKPGDKVTVY GPFGEFFAKD TEAEMVFIGG GAGMAPMRSH IFDQLRRLKS
     NRKISFWYGA RSLREAFYTE EYDQLQAENP NFQWHLALSD PQPEDNWTGL TGFIHNVLFE
     NYLKDHPAPE DCEFYMCGPP MMNAAVIKML TDLGVERENI LLDDFGG
 
 
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