NQRF_MORMI
ID NQRF_MORMI Reviewed; 303 AA.
AC Q9LCI9;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 Moritella marina (Vibrio marinus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Moritellaceae; Moritella.
OX NCBI_TaxID=90736;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15381 / BCRC 15891 / CIP 102861 / NCIMB 1144 / MP-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; AB024726; BAA83763.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9LCI9; -.
DR SMR; Q9LCI9; -.
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; 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; Transport; Ubiquinone.
FT CHAIN <1..>303
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT F"
FT /id="PRO_0000074508"
FT DOMAIN <1..55
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; 34191 MW; 4DF643F69E9D44D5 CRC64;
GGSCGQCRVK VKSGGGDILP TELDHISKGE AREGERLSCQ VSVKVDMDIE LPEEIFGVKK
WECEVISNDN KATFIKELKM AIPNGEVVPF RAGGYIQIEA PAHHVKYSDY DIPEEYRGDW
QHFGFFDVES KVDEDTIRAY SMANCPEEAG IIMLNVRIAT PPPRDLSLPA GKMSSYIFSL
KAGDKVTISG PFGEFFAKET DNEMVFVGGG AGMAPMRSHI FDQLNRLDTK RKVSFWYGAR
SKREMFYVED FDMLAKENEN FEWHVALSDP QPEDNWEGYT GFIHNVILEN YLGNHEAPED
CEY
