ID   ATPB_OLTVI              Reviewed;         481 AA.
AC   Q20EW8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   Oltmannsiellopsis viridis (Marine flagellate) (Oltmannsiella viridis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; Oltmannsiellopsidales;
OC   Oltmannsiellopsidaceae; Oltmannsiellopsis.
OX   NCBI_TaxID=51324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16472375; DOI=10.1186/1741-7007-4-3;
RA   Pombert J.-F., Lemieux C., Turmel M.;
RT   "The complete chloroplast DNA sequence of the green alga Oltmannsiellopsis
RT   viridis reveals a distinctive quadripartite architecture in the chloroplast
RT   genome of early diverging ulvophytes.";
RL   BMC Biol. 4:3-3(2006).
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; DQ291132; ABB81945.1; -; Genomic_DNA.
DR   RefSeq; YP_635877.1; NC_008099.1.
DR   AlphaFoldDB; Q20EW8; -.
DR   SMR; Q20EW8; -.
DR   PRIDE; Q20EW8; -.
DR   GeneID; 4100137; -.
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; Thylakoid;
KW   Translocase; Transport.
FT   CHAIN           1..481
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000254504"
FT   BINDING         162..169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   481 AA;  51501 MW;  DE3E0F8FABF698FB CRC64;
     MNVSVEAKNI GKVVQIIGPV LDVEFSADQM PNIYNAIVVE GENLAGTKVS VTCEVQQLLG
     DHCVRAVSMS ATDGLMRGMD VVDTGAPLTV PVGTSTLGRI FNVLGEPVDN LGDVSNEGGL
     PIHRPAPLFV DLDTQLSIFK TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV LIMELINNIA
     KAHGGVSVFG GVGERTREGN DLYAEMKESK VINEDNLSES KVALVYGQMN EPPGARMRVG
     LTALTMAEYF RDINKQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP TLATEMGGLQ
     ERITSTKDGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRNLAAKG IYPAVDPLDS
     TSTMLQPQTL GEEHYGCAQA VKTTLQRYKE LQDIIAILGL DELSDEDRLV VARARKIERF
     LSQPFFVAEV FTGSPGKYVS LSETIQGFSQ ILTGELDDLP EQSFYLVGNL DEAIAKAATL
     G