NQRF_VIBPA
ID NQRF_VIBPA Reviewed; 407 AA.
AC Q9LCJ0;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 147.
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}; Synonyms=nqr6;
GN OrderedLocusNames=VP2346;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 72-374.
RC STRAIN=JCM 2147;
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: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; BA000031; BAC60609.1; -; Genomic_DNA.
DR EMBL; AB024725; BAA83762.1; -; Genomic_DNA.
DR RefSeq; NP_798725.1; NC_004603.1.
DR RefSeq; WP_005456545.1; NC_004603.1.
DR AlphaFoldDB; Q9LCJ0; -.
DR SMR; Q9LCJ0; -.
DR STRING; 223926.28807344; -.
DR EnsemblBacteria; BAC60609; BAC60609; BAC60609.
DR GeneID; 1189859; -.
DR KEGG; vpa:VP2346; -.
DR PATRIC; fig|223926.6.peg.2249; -.
DR eggNOG; COG2871; Bacteria.
DR HOGENOM; CLU_003827_7_2_6; -.
DR OMA; FIKEFVV; -.
DR Proteomes; UP000002493; Chromosome 1.
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; 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..407
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT F"
FT /id="PRO_0000074509"
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 REGION 272..389
FT /note="Catalytic"
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"
FT CONFLICT 114
FT /note="V -> M (in Ref. 2; BAA83762)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="Q -> E (in Ref. 2; BAA83762)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="I -> V (in Ref. 2; BAA83762)"
FT /evidence="ECO:0000305"
FT CONFLICT 324..326
FT /note="GLA -> MLQ (in Ref. 2; BAA83762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 45083 MW; 747DCC8E99EDBE3A CRC64;
MDIILGVVMF TLIVLALVLV ILFAKSKLVP TGDITISVNG DADKAIVTQP GGKLLSALAG
AGVFVSSACG GGGSCGQCRV KVKSGGGDIL PTELDHITKG EAREGERLAC QVAVKTDMDI
ELPEEIFGVK KWECTVISND NKATFIKELK LQIPDGESVP FRAGGYIQIE APAHHVKYAD
YDIPQEYRED WEKFNLFRYE SKVNEETIRA YSMANYPEEH GIIMLNVRIA TPPPNNPDVP
PGIMSSYIWS LKEGDKCTIS GPFGEFFAKD TDAEMVFIGG GAGMAPMRSH IFDQLKRLHS
KRKMSFWYGA RSKREMFYVE DFDGLAAEND NFVWHCALSD PLPEDNWDGY TGFIHNVLYE
NYLRDHEAPE DCEYYMCGPP MMNAAVIGML KDLGVEDENI LLDDFGG
