(data stored in SCRATCH zone)

SWISSPROT: Q6BME0_DEBHA

ID   Q6BME0_DEBHA            Unreviewed;       503 AA.
AC   Q6BME0;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   11-DEC-2019, entry version 110.
DE   RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE            EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
GN   OrderedLocusNames=DEHA2F06226g {ECO:0000313|EMBL:CAG88959.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 /
OS   IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88959.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88959.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000256|RuleBase:RU003553}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000256|RuleBase:RU003553};
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a, b and c. {ECO:0000256|RuleBase:RU003553}.
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DR   EMBL; CR382138; CAG88959.1; -; Genomic_DNA.
DR   RefSeq; XP_460631.1; XM_460631.1.
DR   STRING; 4959.XP_460631.1; -.
DR   EnsemblFungi; CAG88959; CAG88959; DEHA2F06226g.
DR   GeneID; 2903136; -.
DR   KEGG; dha:DEHA2F06226g; -.
DR   HOGENOM; HOG000009605; -.
DR   InParanoid; Q6BME0; -.
DR   KO; K02133; -.
DR   OMA; FNMIMDG; -.
DR   OrthoDB; 495235at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005754; C:mitochondrial proton-transporting ATP synthase, catalytic core; IEA:EnsemblFungi.
DR   GO; GO:0043531; F:ADP binding; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:EnsemblFungi.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IEA:EnsemblFungi.
DR   Gene3D; 1.10.1140.10; -; 1.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01039; atpD; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BME0.
DR   SWISS-2DPAGE; Q6BME0.
KW   ATP synthesis {ECO:0000256|RuleBase:RU003553};
KW   ATP-binding {ECO:0000256|RuleBase:RU003553};
KW   CF(1) {ECO:0000256|RuleBase:RU003553};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   DOMAIN          174..357
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   503 AA;  53880 MW;  A2EA08370B06F99E CRC64;
     MVFPRLFNSA SRNAFTAAKR NFVFNRGLAS AAPVAGKVRA VIGAVVDIQF DEGNLPAILN
     ALTLKNGDQD LVLEVAQHLG ENTVRAIAMD GTDGLVRGAP VNDTGAPISV PVGRETLGRI
     INVIGEPIDE RGPIKTKQKN PIHADPPSFV EQSTSSEVLE TGIKVVDLLA PYARGGKIGL
     FGGAGVGKTV FIQELINNIA KAHGGFSVFA GVGERTREGN DLYREMQETG VINLEGDSKV
     SLVFGQMNEP PGARARVALT GLTIAEYFRD EEGQDVLLFV DNIYRFTQAG SEVSALLGRI
     PSAVGYQPTL ATDMGLLQER ITTTKKGSVT SVQAVYVPAD DLTDPAPATT FAHLDATTVL
     SRGISELGIY PAVDPLDSKS RLLDIAVVGK EHYDVASGVQ QTLQAYKSLQ DIIAILGMDE
     LSEQDKLTVE RARKIQRFLS QPFAVAEVFT GIPGKLVRLQ ETVKSFKEVL DGKHDHLPEN
     AFYMVGGIED ATAKAEKLAS ESK
//

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