ID A0A2N0WUM5_9GAMM Unreviewed; 843 AA.
AC A0A2N0WUM5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit F {ECO:0000256|ARBA:ARBA00019729};
DE EC=7.2.1.1 {ECO:0000256|ARBA:ARBA00013099};
DE AltName: Full=NQR complex subunit F {ECO:0000256|ARBA:ARBA00030787};
DE AltName: Full=NQR-1 subunit F {ECO:0000256|ARBA:ARBA00030032};
GN Name=nqrF {ECO:0000313|EMBL:PKF59436.1};
GN ORFNames=CW748_01300 {ECO:0000313|EMBL:PKF59436.1};
OS Alteromonadales bacterium alter-6D02.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX NCBI_TaxID=2058087 {ECO:0000313|EMBL:PKF59436.1, ECO:0000313|Proteomes:UP000233605};
RN [1] {ECO:0000313|EMBL:PKF59436.1, ECO:0000313|Proteomes:UP000233605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alter-6D02 {ECO:0000313|Proteomes:UP000233605};
RX PubMed=27311813; DOI=.1038/ncomms11965;
RA Datta M.S., Sliwerska E., Gore J., Polz M.F., Cordero O.X.;
RT "Microbial interactions lead to rapid micro-scale successions on model
RT marine particles.";
RL Nat. Commun. 7:11965-11965(2016).
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}.
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};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000256|ARBA:ARBA00011309}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004533}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the NqrF family.
CC {ECO:0000256|ARBA:ARBA00005570}.
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:PKF59436.1}.
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DR EMBL; PIZK01000002; PKF59436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0WUM5; -.
DR OrthoDB; 9806195at2; -.
DR Proteomes; UP000233605; 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: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 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 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; IPR005625; PepSY-ass_TM.
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 Pfam; PF03929; PepSY_TM; 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};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000233605};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000313|EMBL:PKF59436.1}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 467..561
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 564..704
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 843 AA; 94991 MW; 7FC74F3D77FA9E0E CRC64;
MSNHSSWSTR IRQTHKWLGL IIGLQLCLWV ISGLYMSFID LDKIHGKHLY RTSTNIIAPA
TVSPLPDTYD DISQLTLTQA LGQAIYIIEQ SSQQIVVNAT TLSPLVIDQA YIQAQASDLY
TGTGAIESIE KLAQYPAELG GRKQPIWQVN FNDSFNPSLY FSATTGQFIK ARSDLWRWFD
IMWMLHIMDY QERSDVNNKL LTLASSLAFL ALCSGIWLLF YSFSSVPKPQ AGSLMWLRTA
HKWVAGLIGI QLILWVVSGL VFNWFTSEQI NPRHQLLPQV TQPFKARDID ITQLLSTQSA
IYHIAITATP NASQVIINQQ YQQPLSVDTQ ALTPLSQAQA INVADRVYFS LHDITSTQLI
RESHALTETR KFKRAVWQIN YADVAQHSLY LDAYTGQALT LKNDDWRLKD WFWMLHIMDY
QTRSDFNNPL LITIASIASF SALSGFLMLF YVFSTKDFRF KRQPKSHQIG IYSATQLIET
ITVQSDKPLL AALAEQDVQL PSGCGGGGTC CQCMIKTSNL ITPLNTQEQS SLSVSEMNQG
YRLACQIQAC ENLNIELPQS SLTQQQITAR VISNAFLTPF IKELVIELPA NSSFSFDAGQ
FVNIQVPAYQ QSFSQLSIPA QYRGYWQQQR LLSARVSAEQ PLMRSYSIAT SAHNQGHIQR
LTFIVKLALP QAGYGLGLAS SYLFGLAAGS PLTLSGPLGD FVERQHNLRE MVLIGGGSGM
APLRSHIDTA LAQHPLRQVS LWFGARHQDD IFYQDHFEQL ARKHRNFAWH VSLSQPQGND
WAGKQGHIQT HLFNDYLNQH PRLHLCDFFL CGPPAMMRDI TRLLRAKGIL ETQIRCDDFG
APQ
//
