ID   ATPB_EMIHU              Reviewed;         476 AA.
AC   Q4G3C8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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};
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OG   Plastid; Chloroplast.
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCMP373 / CSIRO-CS-57 / BT6;
RX   PubMed=16408243; DOI=10.1007/s00239-004-0365-4;
RA   Bachvaroff T.R., Sanchez-Puerta M.V., Delwiche C.F.;
RT   "Rate variation as a function of gene origin in plastid-derived genes of
RT   peridinin-containing dinoflagellates.";
RL   J. Mol. Evol. 62:42-52(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP373 / CSIRO-CS-57 / BT6;
RX   PubMed=16303746; DOI=10.1093/dnares/12.2.151;
RA   Sanchez-Puerta M.V., Bachvaroff T.R., Delwiche C.F.;
RT   "The complete plastid genome sequence of the haptophyte Emiliania huxleyi:
RT   a comparison to other plastid genomes.";
RL   DNA Res. 12:151-156(2005).
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; AY675517; AAU81899.1; -; Genomic_DNA.
DR   EMBL; AY741371; AAX13838.1; -; Genomic_DNA.
DR   RefSeq; YP_277339.1; NC_007288.1.
DR   AlphaFoldDB; Q4G3C8; -.
DR   SMR; Q4G3C8; -.
DR   PRIDE; Q4G3C8; -.
DR   GeneID; 3562515; -.
DR   Proteomes; UP000013827; Unassembled WGS sequence.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
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   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..476
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000254472"
FT   BINDING         155..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   476 AA;  50767 MW;  D79707708DCFF44C CRC64;
     MVDTASKTGF ISQIIGPVVD VEFPGGELPT VYSAIVVGEG ESSVTCEVQQ LLGSNKVRAV
     SMTSTDGLKR GAAVVNTGAP ITVPVGVPTL GRIFNVLGEP VDEMGPCEAT AGLPIHRAAP
     AFTDLDTKPS VFETGIKVVD LLAPYKRGGK IGLFGGAGVG KTVLIMELIN NIARAHGGVS
     VFGGVGERTR EGNDLYAEMK ESGVIDEKKL DNSKVALVYG QMNEPPGARM RVGLTALTMA
     EYFRDVNKQD VLLFIDNIFR FVQAGSEVSA LLGRMPSAVG YQPTLATEMG VLQERITSTT
     EGSITSIQAV YVPADDLTDP APATTFAHLD ATTVLSRGLA SKGIYPAVDP LDSTSTMLQP
     EIVGAEHYAT AQNIKETLQR YKELQDIIAI LGLDELSEED RLTVARARKV ERFLSQPFFV
     AEVFTGSPGK YVSLADSIDG FNRLLDGEFD DLPEQSFYLV GDINEAIEKA AKINAK