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ATPB_OSTTA
ID   ATPB_OSTTA              Reviewed;         483 AA.
AC   Q0P3P2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=ATP synthase subunit beta, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01347};
DE            EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE   AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE   AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN   Name=atpB {ECO:0000255|HAMAP-Rule:MF_01347}; OrderedLocusNames=OtCpg00100;
OS   Ostreococcus tauri.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=70448;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OTTH0595;
RX   PubMed=17251180; DOI=10.1093/molbev/msm012;
RA   Robbens S., Derelle E., Ferraz C., Wuyts J., Moreau H., Van de Peer Y.;
RT   "The complete chloroplast and mitochondrial DNA sequence of Ostreococcus
RT   tauri: organelle genomes of the smallest eukaryote are examples of
RT   compaction.";
RL   Mol. Biol. Evol. 24:956-968(2007).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The catalytic sites are hosted primarily by the
CC       beta subunits. {ECO:0000255|HAMAP-Rule:MF_01347}.
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:0000255|HAMAP-Rule:MF_01347};
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 four main
CC       subunits: a(1), b(1), b'(1) and c(9-12). {ECO:0000255|HAMAP-
CC       Rule:MF_01347}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01347}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01347}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR   EMBL; CR954199; CAL36335.1; -; Genomic_DNA.
DR   RefSeq; YP_717213.1; NC_008289.1.
DR   AlphaFoldDB; Q0P3P2; -.
DR   SMR; Q0P3P2; -.
DR   STRING; 70448.Q0P3P2; -.
DR   GeneID; 4238808; -.
DR   KEGG; ota:OstapCp10; -.
DR   eggNOG; KOG1350; Eukaryota.
DR   InParanoid; Q0P3P2; -.
DR   OrthoDB; 495235at2759; -.
DR   Proteomes; UP000009170; Chloroplast.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
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-UniRule.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
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   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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;
KW   ATP synthesis; ATP-binding; CF(1); Chloroplast; Hydrogen ion transport;
KW   Ion transport; Membrane; Nucleotide-binding; Plastid; Reference proteome;
KW   Thylakoid; Translocase; Transport.
FT   CHAIN           1..483
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000254506"
FT   BINDING         163..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   483 AA;  51862 MW;  87146B93662B603C CRC64;
     MTALKTEQNI GRITQIIGPV IDAVFSPNKM PNIYNSVVIE GKNDVGDTIK CVAEVQQLLG
     DNVVRAVSMS ATDGLMRGMT VVDTGAALSV PVGKNTLGRI FNVLGEPVDE LGAVSTPEGM
     LPIHRAAPAF VDLDTNLSIF ETGIKVVDLL APYRRGGKIG LFGGAGVGKT VLIMELIVNN
     NIAKAHGGVS VFAGVGERTR EGNDLYQEMC ESKVIDTANL ANSKVALVYG QMNEPPGARM
     RVGLTALTMA EYFRDVNNQD VLLFVDNIFR FVQAGSEVSA LLGRMPSAVG YQPTLSTEMG
     SLQERITSTK TGSITSIQAV YVPADDLTDP APATTFAHLD ATTVLSRNLA AKGIYPAVDP
     LDSTSTMLQP WILGDDHYDT AQGVKQTLQR YKELQDIIAI LGLDELSEED RLTVARARKV
     ERFLSQPFFV AEVFTGSPGK YVSLAESIQG FKMILGGELD DLPEQAFYLV GNIDEAVEKA
     AKL
 
 
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