位置:首页 > 蛋白库 > NQRF_PSEAE
NQRF_PSEAE
ID   NQRF_PSEAE              Reviewed;         407 AA.
AC   Q9HZL1;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Na(+)-translocating NADH-quinone reductase subunit F {ECO:0000255|HAMAP-Rule:MF_00430};
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};
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}; OrderedLocusNames=PA2994;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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}.
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};
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   -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC       NqrF. {ECO:0000255|HAMAP-Rule:MF_00430}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00430}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00430}.
CC   -!- SIMILARITY: Belongs to the NqrF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00430}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004091; AAG06382.1; -; Genomic_DNA.
DR   PIR; C83272; C83272.
DR   RefSeq; NP_251684.1; NC_002516.2.
DR   RefSeq; WP_003113984.1; NZ_CP053028.1.
DR   AlphaFoldDB; Q9HZL1; -.
DR   SMR; Q9HZL1; -.
DR   STRING; 287.DR97_4944; -.
DR   PaxDb; Q9HZL1; -.
DR   PRIDE; Q9HZL1; -.
DR   EnsemblBacteria; AAG06382; AAG06382; PA2994.
DR   GeneID; 878840; -.
DR   KEGG; pae:PA2994; -.
DR   PATRIC; fig|208964.12.peg.3142; -.
DR   PseudoCAP; PA2994; -.
DR   HOGENOM; CLU_003827_7_2_6; -.
DR   InParanoid; Q9HZL1; -.
DR   OMA; FIKEFVV; -.
DR   PhylomeDB; Q9HZL1; -.
DR   BioCyc; PAER208964:G1FZ6-3046-MON; -.
DR   PHI-base; PHI:8940; -.
DR   Proteomes; UP000002438; Chromosome.
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; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
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   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; 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   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   3: Inferred from homology;
KW   2Fe-2S; Cell inner membrane; Cell membrane; FAD; Flavoprotein;
KW   Ion transport; Iron; Iron-sulfur; Membrane; Metal-binding; NAD;
KW   Reference proteome; 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_0000074501"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   DOMAIN          35..127
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   DOMAIN          130..269
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   REGION          272..389
FT                   /note="Catalytic"
FT   BINDING         70
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   BINDING         76
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   BINDING         79
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
FT   BINDING         111
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00430"
SQ   SEQUENCE   407 AA;  45471 MW;  1D6EEEAFBDB99244 CRC64;
     MIGFEIFLAI GMFTAIVLGL VAIILVARAK LVSSGDVTIQ INGEHSLTVP AGGKLLQTLA
     ANNVFLSSAC GGGGTCAQCK CVVVEGGGEM LPTEESHFTR RQAKEGWRLS CQTPVKQDMQ
     IRVPEEVFGV KKWECTVESN PNVATFIKEL TLRLPDGESV DFRAGGYVQL ECPPHVVEYK
     DFDIQPEYRG DWDKFNMWRY VSKVDETVIR AYSMANYPEE KGVVKFNIRI ASPPPGSDLP
     PGQMSSWVFN LKPGDKVTVY GPFGEFFAKD TEAEMVFIGG GAGMAPMRSH IFDQLRRLKS
     NRKISFWYGA RSLREAFYTE EYDQLQAENP NFQWHLALSD PQPEDNWTGL TGFIHNVLFE
     NYLKDHPAPE DCEFYMCGPP MMNAAVIKML TDLGVERENI LLDDFGG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024