ID A0A090VEC9_9FLAO Unreviewed; 438 AA.
AC A0A090VEC9; A0A4R8MBA8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=DFQ06_2770 {ECO:0000313|EMBL:TDY61437.1}, JCM19300_1119
GN {ECO:0000313|EMBL:GAL63101.1};
OS Algibacter lectus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Algibacter.
OX NCBI_TaxID=221126 {ECO:0000313|EMBL:GAL63101.1, ECO:0000313|Proteomes:UP000029644};
RN [1] {ECO:0000313|EMBL:GAL63101.1, ECO:0000313|Proteomes:UP000029644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19300 {ECO:0000313|EMBL:GAL63101.1,
RC ECO:0000313|Proteomes:UP000029644};
RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K.,
RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., Niwa A.,
RA Sawabe T., Sawabe T.;
RT "Draft Genome Sequences of Marine Flavobacterium Algibacter lectus Strains
RT SS8 and NR4.";
RL Genome Announc. 2:e01168-14(2014).
RN [2] {ECO:0000313|EMBL:TDY61437.1, ECO:0000313|Proteomes:UP000294824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8301 {ECO:0000313|EMBL:TDY61437.1,
RC ECO:0000313|Proteomes:UP000294824};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAL63101.1}.
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DR EMBL; BBNQ01000009; GAL63101.1; -; Genomic_DNA.
DR EMBL; SORL01000009; TDY61437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090VEC9; -.
DR Proteomes; UP000029644; Unassembled WGS sequence.
DR Proteomes; UP000294824; Unassembled WGS sequence.
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; cd00207; fer2; 1.
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; 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 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 PRINTS; PR00371; FPNCR.
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:UP000029644};
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00430};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00430}; Transport {ECO:0000256|HAMAP-Rule:MF_00430};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|HAMAP-
KW Rule:MF_00430}.
FT TRANSMEM 6..35
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
FT DOMAIN 43..135
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 138..290
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 78
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
FT BINDING 84
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
FT BINDING 87
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
FT BINDING 119
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
SQ SEQUENCE 438 AA; 48918 MW; 0962FF17C708C233 CRC64;
MSNMILAAST IGTIGVTVIA FLIILLLLVG LLLVVKQKLS PSGPVKITIN GEKEIEVASG
ASLLSTLGNS KIFLPSACGG GGTCIQCECH VNSGGGEALP TEVPHFTRKE LQHGARLACQ
VKVKQDMDIT IPEEVFGIKK WEAVVVRNYN VASFIKEFVV EIPEDMGYKA GGYIQIEIPP
CEVKYSDMDI TAHPEEHETP DKFQAEWDKF KLWPLVMKNT ETIERAYSMA SYPAEGREIM
LNVRVACPPF DRAKGGWMDV NPGIASSYIF NQKPGDKVTI SGPYGEFFIN ESESEMLYVG
GGAGMAPMRS HLYHLFKTLK TGRKVTYWYG GRSKRELFYL EHFYELEKEF PNFKFYLALS
EPMEEDNWKV KENIDAPGDG FVGFIHNCVI DNYLSLHESP EDIELYFCGP PLMNKAVQKM
GEDFGIPDEH IRFDDFGG
//
