ID Q8I0V2_PLAF7 Unreviewed; 535 AA.
AC Q8I0V2;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 151.
DE RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
GN ORFNames=PF3D7_1235700 {ECO:0000313|EMBL:CZT99516.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000313|EMBL:CZT99516.1, ECO:0000313|Proteomes:UP000001450};
RN [1] {ECO:0000313|EMBL:CZT99516.1, ECO:0000313|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., Chan M.S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
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}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
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DR EMBL; LN999947; CZT99516.1; -; Genomic_DNA.
DR RefSeq; XP_001350751.1; XM_001350715.1.
DR AlphaFoldDB; Q8I0V2; -.
DR SMR; Q8I0V2; -.
DR IntAct; Q8I0V2; 1.
DR STRING; 36329.Q8I0V2; -.
DR TCDB; 3.A.2.1.16; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR SwissPalm; Q8I0V2; -.
DR PaxDb; 5833-PFL1725w; -.
DR EnsemblProtists; CZT99516; CZT99516; PF3D7_1235700.
DR GeneID; 811397; -.
DR KEGG; pfa:PF3D7_1235700; -.
DR VEuPathDB; PlasmoDB:PF3D7_1235700; -.
DR HOGENOM; CLU_022398_0_2_1; -.
DR InParanoid; Q8I0V2; -.
DR OMA; GFNMIMD; -.
DR OrthoDB; 3420200at2759; -.
DR PhylomeDB; Q8I0V2; -.
DR Proteomes; UP000001450; Chromosome 12.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:GeneDB.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; ISS:GeneDB.
DR CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01039; atpD; 1.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039072; ATPase_subunit_beta; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW ECO:0000256|RuleBase:RU003553};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003553};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003553};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Hydrolase {ECO:0000313|EMBL:CZT99516.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003553}; Plastid {ECO:0000256|ARBA:ARBA00022528};
KW Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 197..475
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 535 AA; 58394 MW; BBB69DD5876BBBC8 CRC64;
MHKLKLFNHW KKLPMFMKFG GSPNLRMNCR YVSSSEHLNM KKNISVGNKN TEVSNKIKIG
KIAQVIGAVV DVEFEDTPPS ILNALEVELD NKKLILEVAQ HLGNKVVRTI AMDATDGLVR
GQEVKDSGNP ICVPVGKETL GRIMNVIGEP IDECGHINHK KTLPIHRDPP LFTDQSTEPA
LLITGIKVVD LIAPYAKGGK IGLFGGAGVG KTVLIMELIN NVAKKHGGYS VFAGVGERTR
EGNDLYHEMI TTGVIKKKKI GNNEFDFNGS KAALVYGQMN EPPGARARVA LTGLTVAEYF
RDEENQDVLL FIDNIYRFTQ AGSEVSALLG RIPSAVGYQP TLATDLGALQ ERITTTKNGS
ITSVQAVYVP ADDLTDPAPA TTFSHLDATT VLSRSIAELG IYPAVDPLDS TSRMLTPDIV
GAEQYQVARN VQQILQDYKS LQDIIAILGI DELSEQDKLT VARARKVQRF LSQPFAVAEV
FTGKPGRFVE LEDTIIGFSE LLKGNCDDLP EMAFYMVGGL EEVKSKALEM AKQVS
//
