ID R7JGK4_9BACT Unreviewed; 420 AA.
AC R7JGK4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=BN752_01636 {ECO:0000313|EMBL:CDE62871.1};
OS Alistipes putredinis CAG:67.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1263036 {ECO:0000313|EMBL:CDE62871.1, ECO:0000313|Proteomes:UP000018026};
RN [1] {ECO:0000313|EMBL:CDE62871.1, ECO:0000313|Proteomes:UP000018026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:67 {ECO:0000313|Proteomes:UP000018026};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE62871.1}.
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DR EMBL; CBJI010000010; CDE62871.1; -; Genomic_DNA.
DR AlphaFoldDB; R7JGK4; -.
DR Proteomes; UP000018026; 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; 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:UP000018026};
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..26
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
FT DOMAIN 34..127
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 130..276
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 70
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
FT BINDING 76
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
FT BINDING 79
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
FT BINDING 111
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00430"
SQ SEQUENCE 420 AA; 46653 MW; 962E76D825EA7EE6 CRC64;
MTLTIIIAIV AFLVITLILV GLLLFAKAKL TTSGDVTIDI NGGEKVLIAE SGGTLLSTLA
NNNVFLPSAC GGGGSCGMCK CQVLEGGGEL LPTETGFINR KMAKEHWRLG CQVKVKENLK
IHVPESVLGV KKWECEVISN RNISTFLKEF VVKLPEGENL KFRSGGYIQI DIPKYDAIKF
SDMDIEEPYR EDWDKMKMWD LVTKNPEPTF RAYSMANHPA EGNIIMLNIR IATPPFDRAT
GTFAKVNPGI CSSYIFSRKP GDKVTISGPY GEFFLPDNLP ATQELVFIGG GAGMAPMRSH
IMHLFKTEKT SRPVSFWYGA RALKEVPYMD EFLEIQREFP NFKFHLALDR PDPQADAAGV
KYTPGFVHNV LYENYLKNHQ APEDNIYLMC GPPMMISSVV KMLDSLGVPS ENILYDNFGS
//
