NQRF_VIBAL
ID NQRF_VIBAL Reviewed; 407 AA.
AC Q56584;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit F {ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000303|PubMed:9490015};
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, ECO:0000269|PubMed:9490015};
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};
GN Synonyms=nqr6 {ECO:0000303|PubMed:7729558};
OS Vibrio alginolyticus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7729558; DOI=10.1016/0014-5793(95)00283-f;
RA Hayashi M., Hirai K., Unemoto T.;
RT "Sequencing and the alignment of structural genes in the nqr operon
RT encoding the Na(+)-translocating NADH-quinone reductase from Vibrio
RT alginolyticus.";
RL FEBS Lett. 363:75-77(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8674603; DOI=10.1042/bst024012s;
RA Tan K., Beattie P., Leach D.R.F., Rich P.R., Coulson A.F.W., Ward F.B.;
RT "Expression and analysis of the gene for the catalytic beta subunit of the
RT sodium-translocating NADH-ubiquinone oxidoreductase of Vibrio
RT alginolyticus.";
RL Biochem. Soc. Trans. 24:12S-12S(1996).
RN [3]
RP PROTEIN SEQUENCE OF 1-10, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=9490015; DOI=10.1016/s0014-5793(98)00016-7;
RA Nakayama Y., Hayashi M., Unemoto T.;
RT "Identification of six subunits constituting Na+-translocating NADH-quinone
RT reductase from the marine Vibrio alginolyticus.";
RL FEBS Lett. 422:240-242(1998).
RN [4]
RP COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 17749 / DSM 2171 / NBRC 15630 / NCIMB 1903 / XII-53;
RX PubMed=9395325; DOI=10.1111/j.1432-1033.1997.t01-2-00770.x;
RA Steuber J., Krebs W., Dimroth P.;
RT "The Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio
RT alginolyticus -- redox states of the FAD prosthetic group and mechanism of
RT Ag+ inhibition.";
RL Eur. J. Biochem. 249:770-776(1997).
RN [5]
RP INHIBITION OF ENZYMATIC ACTIVITY.
RA Unemoto T., Ogura T., Hayashi M.;
RT "Modifications by Na+ and K+, and the site of Ag+ inhibition in the Na+-
RT translocating NADH-quinone reductase from a marine Vibrio alginolyticus.";
RL Biochim. Biophys. Acta 1183:201-205(1993).
RN [6]
RP INHIBITION OF ENZYMATIC ACTIVITY.
RX PubMed=10549856; DOI=10.1248/bpb.22.1064;
RA Nakayama Y., Hayashi M., Yoshikawa K., Mochida K., Unemoto T.;
RT "Inhibitor studies of a new antibiotic, korormicin, 2-n-heptyl-4-
RT hydroxyquinoline N-oxide and Ag+ toward the Na+-translocating NADH-quinone
RT reductase from the marine Vibrio alginolyticus.";
RL Biol. Pharm. Bull. 22:1064-1067(1999).
RN [7]
RP REVIEW.
RX PubMed=11248187; DOI=10.1016/s0005-2728(00)00275-9;
RA Hayashi M., Nakayama Y., Unemoto T.;
RT "Recent progress in the Na(+)-translocating NADH-quinone reductase from the
RT marine Vibrio alginolyticus.";
RL Biochim. Biophys. Acta 1505:37-44(2001).
RN [8]
RP REVIEW.
RX PubMed=11248188; DOI=10.1016/s0005-2728(00)00276-0;
RA Steuber J.;
RT "Na(+) translocation by bacterial NADH:quinone oxidoreductases: an
RT extension to the complex-I family of primary redox pumps.";
RL Biochim. Biophys. Acta 1505:45-56(2001).
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, ECO:0000305|PubMed:11248187,
CC ECO:0000305|PubMed:11248188}.
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, ECO:0000269|PubMed:9490015};
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 ECO:0000269|PubMed:9395325};
CC -!- ACTIVITY REGULATION: Activated by Na(+) or K(+). Inhibited by silver.
CC {ECO:0000269|PubMed:10549856, ECO:0000269|PubMed:9395325,
CC ECO:0000269|Ref.5}.
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000269|PubMed:9490015}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00430, ECO:0000305}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00430}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:9490015}.
CC -!- SIMILARITY: Belongs to the NqrF family. {ECO:0000255|HAMAP-
CC Rule:MF_00430, ECO:0000305}.
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DR EMBL; AB008030; BAA22915.1; -; Genomic_DNA.
DR PIR; S65531; S65531.
DR RefSeq; WP_005380271.1; NZ_WAHT01000008.1.
DR AlphaFoldDB; Q56584; -.
DR SMR; Q56584; -.
DR STRING; 663.BAU10_10815; -.
DR TCDB; 3.D.5.1.1; the na(+)-translocating nadh:quinone dehydrogenase (na-ndh or nqr) family.
DR GeneID; 61533192; -.
DR eggNOG; COG2871; Bacteria.
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; ISS:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
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; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 2Fe-2S; Cell inner membrane; Cell membrane; Direct protein sequencing; FAD;
KW Flavoprotein; Ion transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW NAD; 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_0000074504"
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"
SQ SEQUENCE 407 AA; 45275 MW; A878E89DFCA87346 CRC64;
MDIILGVVMF TLIVLALVLV ILFAKSKLVP TGDITISVND DPSLAIVTQP GGKLLSALAG
AGVFVSSACG GGGSCGQCRV KVKSGGGDIL PTELDHITKG EAREGERLAC QVAMKTDMDI
ELPEEIFGVK KWECTVISND NKATFIKELK LQIPDGESVP FRAGGYIQIE APAHHVKYAD
YDIPEEYRED WEKFNLFRYE SKVNEETIRA YSMANYPEEH GIIMLNVRIA TPPPNNPDVP
PGIMSSYIWS LKEGDKCTIS GPFGEFFAKD TDAEMVFVGG GAGMAPMRSH IFDQLKRLHS
KRKMSFWYGA RSKREMFYVE DFDMLQAEND NFVWHCALSD PLPEDNWDGY TGFIHNVLYE
NYLRDHEAPE DCEYYMCGPP MMNAAVIGML KDLGVEDENI LLDDFGG
