NQRF_ACTP2
ID NQRF_ACTP2 Reviewed; 409 AA.
AC A3MYM7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=APL_0155;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN73263.1; -; Genomic_DNA.
DR RefSeq; WP_005595870.1; NC_009053.1.
DR AlphaFoldDB; A3MYM7; -.
DR SMR; A3MYM7; -.
DR STRING; 416269.APL_0155; -.
DR EnsemblBacteria; ABN73263; ABN73263; APL_0155.
DR GeneID; 66258997; -.
DR KEGG; apl:APL_0155; -.
DR eggNOG; COG2871; Bacteria.
DR HOGENOM; CLU_003827_7_2_6; -.
DR OMA; FIKEFVV; -.
DR Proteomes; UP000001432; 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..409
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT F"
FT /id="PRO_1000080572"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT DOMAIN 34..128
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT DOMAIN 131..271
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT BINDING 71
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT BINDING 77
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT BINDING 80
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT BINDING 112
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
SQ SEQUENCE 409 AA; 45509 MW; DE61E2A30E2D01F5 CRC64;
MDSNFIFGII AFTALVLVLA VIILFAKSKL VDSGDITISI NNDPEKGITL PAGGKLLGAL
ASKGIFVSSA CGGGGSCGQC KVQVKSGGGE ILPTELSHIS KKEAKEGWRL ACQVNVKSSM
DVELPEEIFG VKKWECTVIS NDNKATFIKE LKLQIPEGEE VPFRAGGYIQ IEADPHTVNY
KDFDIPKEYH EDWDKFNLWR YVSKVDEHII RAYSMASYPE EKGIIMLNVR IATPPPRNPD
VPPGQMSSYI WSLKPGDKVT ISGPFGEFFA KETDNEMVFI GGGAGMAPMR SHIFDQLKRL
KSKRKMSFWY GARSKREIFY QEDFDQLAAE NDNFVWHVAL SDALPEDNWT GYTGFIHNVL
YENYLKNHEA PEDCEYYMCG PPVMNAAVIG MLKSLGVEDE NILLDDFGG
