(data stored in SCRATCH zone)

SWISSPROT: A4ATH2_MARSH

ID   A4ATH2_MARSH            Unreviewed;       435 AA.
AC   A4ATH2;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Na(+)-translocating NADH-quinone reductase subunit F {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|HAMAP-Rule:MF_00430};
DE   AltName: Full=NQR complex subunit F {ECO:0000256|HAMAP-Rule:MF_00430};
DE   AltName: Full=NQR-1 subunit F {ECO:0000256|HAMAP-Rule:MF_00430};
GN   Name=nqrF {ECO:0000256|HAMAP-Rule:MF_00430};
GN   OrderedLocusNames=FB2170_16696 {ECO:0000313|EMBL:EAR00742.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00742.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00742.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to
CC       ubiquinol by two successive reactions, coupled with the transport
CC       of Na(+) ions from the cytoplasm to the periplasm. The first step
CC       is catalyzed by NqrF, which accepts electrons from NADH and
CC       reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer
CC       pathway. {ECO:0000256|HAMAP-Rule:MF_00430}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol +
CC         n Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-
CC         COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.2.1.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00430};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00430};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
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
CC       and NqrF. {ECO:0000256|HAMAP-Rule:MF_00430}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00430}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00430}.
CC   -!- SIMILARITY: Belongs to the NqrF family. {ECO:0000256|HAMAP-
CC       Rule:MF_00430}.
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DR   EMBL; CP002157; EAR00742.1; -; Genomic_DNA.
DR   RefSeq; WP_013304545.1; NC_014472.1.
DR   STRING; 313603.FB2170_16696; -.
DR   EnsemblBacteria; EAR00742; EAR00742; FB2170_16696.
DR   KEGG; fbc:FB2170_16696; -.
DR   eggNOG; ENOG4105D26; Bacteria.
DR   eggNOG; COG2871; LUCA.
DR   HOGENOM; HOG000263661; -.
DR   KO; K00351; -.
DR   OMA; YWYGGRS; -.
DR   OrthoDB; 1834577at2; -.
DR   BioCyc; MSP313603:G1GNS-116-MONOMER; -.
DR   Proteomes; UP000001602; 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: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; 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   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; 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;
DR   PRODOM; A4ATH2.
DR   SWISS-2DPAGE; A4ATH2.
KW   2Fe-2S {ECO:0000256|HAMAP-Rule:MF_00430,
KW   ECO:0000256|SAAS:SAAS00660781};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00430};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00430};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_00430};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00430,
KW   ECO:0000256|SAAS:SAAS01101457};
KW   Ion transport {ECO:0000256|HAMAP-Rule:MF_00430};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00430, ECO:0000256|SAAS:SAAS00909025};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00430,
KW   ECO:0000256|SAAS:SAAS00908250};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00430};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00430,
KW   ECO:0000256|SAAS:SAAS00909276};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00430};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Sodium {ECO:0000256|HAMAP-Rule:MF_00430};
KW   Sodium transport {ECO:0000256|HAMAP-Rule:MF_00430};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_00430};
KW   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|HAMAP-Rule:MF_00430}.
FT   TRANSMEM     12     31       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00430}.
FT   DOMAIN       40    132       2Fe-2S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51085}.
FT   DOMAIN      135    287       FAD-binding FR-type.
FT                                {ECO:0000259|PROSITE:PS51384}.
FT   METAL        75     75       Iron-sulfur (2Fe-2S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00430}.
FT   METAL        81     81       Iron-sulfur (2Fe-2S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00430}.
FT   METAL        84     84       Iron-sulfur (2Fe-2S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00430}.
FT   METAL       116    116       Iron-sulfur (2Fe-2S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00430}.
SQ   SEQUENCE   435 AA;  48753 MW;  4B7B1E33372DD66C CRC64;
     MILATSTGGT ILITVISFLI LLLALVALLL FTKEKLSPSG PVTITINGEK KVEVSSGGSL
     LSTLGNQKIF LPSACGGGGT CIQCECHVLE GGGEALPTET PHFSKRELNE GARLACQVKV
     KQDMNITIPE EVFGIKKWEG TVVRNYNVAS FIKEFVVEIP EDMGYKAGGY IQIEIPPCEI
     KYSDIDITAH PEEHETPDKF QAEWDKFNLW PLVMKNPETV ERAYSMASFP AEGREIMLNV
     RIATPPWDRS KNGWMDVNPG VASSYIFAQK PGDKVVISGP YGEFFINESE SEMLYVGGGA
     GMAPMRSHLY HLFKTLRTNR KVTYWYGGRS KRELFYLDHF YQLEKEFSNF KFYLALSEPM
     EEDNWKVKED IDAPGDGFVG FIHNCVIDNY LSKHESPEDI ELYFCGPPLM NKAVQKMGED
     FGIPDEHIRF DDFGG
//

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