ID A0A1Y0CXU7_9GAMM Unreviewed; 407 AA.
AC A0A1Y0CXU7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit F {ECO:0000256|ARBA:ARBA00019729, ECO:0000256|HAMAP-Rule:MF_00430};
DE Short=Na(+)-NQR subunit F {ECO:0000256|HAMAP-Rule:MF_00430};
DE Short=Na(+)-translocating NQR subunit F {ECO:0000256|HAMAP-Rule:MF_00430};
DE EC=7.2.1.1 {ECO:0000256|ARBA:ARBA00013099, ECO:0000256|HAMAP-Rule:MF_00430};
DE AltName: Full=NQR complex subunit F {ECO:0000256|ARBA:ARBA00030787, ECO:0000256|HAMAP-Rule:MF_00430};
DE AltName: Full=NQR-1 subunit F {ECO:0000256|ARBA:ARBA00030032, ECO:0000256|HAMAP-Rule:MF_00430};
GN Name=nqrF {ECO:0000256|HAMAP-Rule:MF_00430};
GN ORFNames=CBP12_06510 {ECO:0000313|EMBL:ART79844.1};
OS Oceanisphaera avium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Oceanisphaera.
OX NCBI_TaxID=1903694 {ECO:0000313|EMBL:ART79844.1, ECO:0000313|Proteomes:UP000243793};
RN [1] {ECO:0000313|Proteomes:UP000243793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMac2203 {ECO:0000313|Proteomes:UP000243793};
RA Sung H.;
RL Submitted (MAY-2017) 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:0000256|ARBA:ARBA00002972, ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000176, ECO:0000256|HAMAP-
CC Rule:MF_00430};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_00430};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00430};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000256|HAMAP-Rule:MF_00430};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000256|ARBA:ARBA00011309, ECO:0000256|HAMAP-Rule:MF_00430}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00430};
CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00430}.
CC -!- SIMILARITY: Belongs to the NqrF family. {ECO:0000256|ARBA:ARBA00005570,
CC ECO:0000256|HAMAP-Rule:MF_00430}.
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DR EMBL; CP021376; ART79844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0CXU7; -.
DR KEGG; ocm:CBP12_06510; -.
DR OrthoDB; 9806195at2; -.
DR Proteomes; UP000243793; Chromosome.
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: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; cd06188; NADH_quinone_reductase; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR010205; NqrF.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR NCBIfam; TIGR01941; nqrF; 1.
DR PANTHER; PTHR43644; NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR43644:SF1; NAD(P)H-FLAVIN REDUCTASE; 1.
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 SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|HAMAP-Rule:MF_00430};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00430};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00430};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00430};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_00430};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00430};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00430};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00430};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00430};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00430};
KW Reference proteome {ECO:0000313|Proteomes:UP000243793};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|HAMAP-Rule:MF_00430};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201, ECO:0000256|HAMAP-
KW Rule:MF_00430};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_00430}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_00430};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00430};
KW Transport {ECO:0000256|HAMAP-Rule:MF_00430};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|HAMAP-
KW Rule:MF_00430}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
FT DOMAIN 32..126
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 129..269
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 69
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
FT BINDING 75
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
FT BINDING 110
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
SQ SEQUENCE 407 AA; 45442 MW; F9293F41F2534519 CRC64;
MEIILGVVMF TVIVLVLVGI ILFAKSKLVE EGDVVISIND DPDKTITTSA GGKLLGALAN
NGIFVSSACG GGGTCGQCRV RILDGGGEIL PTELDHISKG EARHGERLSC QVNVKQNMKI
ELPEEVFGIK KWDCEVLSND SKATFIKELK LKIPNGESVP FRAGGYIQIE APPHHVKYKD
FDVPEKFRED WDKFKIFELE SKVDEETIRA YSMANYPEEE GMILLNVRIA TPPPRNWDAP
PGKMSSYIWS LKPGDKATIS GPFGEFFAKD TDAEMVFVGG GAGMAPMRSH IFDQLKRLDS
KRKISFWYGA RSRREMFYVE DFDGLAAEHD NFTWHVALSD STPEDEWTGY TGFIHNVLYE
NYLRDHEAPE DCEYYMCGPP VMNAAVINML KDLGVEEENI LLDDFGG
//
