NQRF_SERP5
ID NQRF_SERP5 Reviewed; 407 AA.
AC A8GAC4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Spro_0958;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) 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; CP000826; ABV40064.1; -; Genomic_DNA.
DR RefSeq; WP_012005401.1; NC_009832.1.
DR AlphaFoldDB; A8GAC4; -.
DR SMR; A8GAC4; -.
DR STRING; 399741.Spro_0958; -.
DR EnsemblBacteria; ABV40064; ABV40064; Spro_0958.
DR KEGG; spe:Spro_0958; -.
DR eggNOG; COG2871; Bacteria.
DR HOGENOM; CLU_003827_7_2_6; -.
DR OMA; FIKEFVV; -.
DR OrthoDB; 1834577at2; -.
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; 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_1000080593"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT DOMAIN 32..126
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT DOMAIN 129..269
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT BINDING 69
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT BINDING 75
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT BINDING 110
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
SQ SEQUENCE 407 AA; 45415 MW; 4E50BEC546269100 CRC64;
MEIILGVAMF TGIVMVLVLL ILFAKSRLVN TGDIAVEVNG DLDKSFTAPA GDKLLNMLSS
QGIFVSSACG GGGSCGQCRV VIKEGGGDIL PTELSHINKR EAKEGCRLAC QVNVKQNLKI
ELPEEIFGVK KWECEVISND NKATFIKELK LKIPDGEDVP FRAGGFIQIE APAHDISYAD
FDVPDEYRGD WDKFNLFRYR SVVNETTVRA YSMANYPDEK GIIMLNVRIA TPPPRDPDVP
PGIMSSYIWS LKAGDKVTIS GPFGEFFAKD TDAEMIFIGG GAGMAPMRSH IFDQLNRLKS
KRKITFWYGA RSLREMFYEE DFNQLQAENE NFTWHVALSD PQPEDNWTGY TGFIHNVLLE
NYLRNHPAPE DCEFYMCGPP MMNAAVIKML KDLGVEDENI MLDDFGG
