ID   ATPB_TETOB              Reviewed;         480 AA.
AC   Q1KVT0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
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   Tetradesmus obliquus (Green alga) (Acutodesmus obliquus).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Scenedesmaceae; Tetradesmus.
OX   NCBI_TaxID=3088;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 393;
RX   PubMed=16638149; DOI=10.1186/1471-2148-6-37;
RA   de Cambiaire J.-C., Otis C., Lemieux C., Turmel M.;
RT   "The complete chloroplast genome sequence of the chlorophycean green alga
RT   Scenedesmus obliquus reveals a compact gene organization and a biased
RT   distribution of genes on the two DNA strands.";
RL   BMC Evol. Biol. 6:37-37(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; DQ396875; ABD48277.1; -; Genomic_DNA.
DR   RefSeq; YP_635994.1; NC_008101.1.
DR   AlphaFoldDB; Q1KVT0; -.
DR   SMR; Q1KVT0; -.
DR   GeneID; 4099783; -.
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..480
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000254522"
FT   BINDING         161..168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   480 AA;  51771 MW;  60FE110B735B234F CRC64;
     MSDLNTKNVG KISQIIGPVL DIAFGQGQVP NIYNALTIKA KNAAGLEMSV TCEVQQLLGD
     SCVRAVAMNP TDGLMRGMEV LDTGKPLNVP VGKSTLGRIF NVLGEPVDNL GPVKNEESLP
     IHRTAPAFVD LDTRLSIFET GIKVVDLLAP YRRGGKIGLF GGAGVGKTVL IMELINNIAK
     AHGGVSVFAG VGERTREGND LYTEMKESGV IVEKNLIDSK VALVYGQMNE PPGARMRVAL
     TALTMAEYFR DVNKQDVLFF IDNIFRFVQA GAEVSALLGR MPSAVGYQPT LATEMGALQE
     RITSTKDGSI TSIQAVYVPA DDLTDPAPAT TFAHLDATTV LSRGLASKGI YPAVDPLDST
     STMLQPWILG EKHYGCAQSV KRTLQRYKEL QDIIAILGLD ELSEEDRLVV ARARKIERFL
     SQPFFVAEVF TGSPGKYVSL AETIEGFNKI LAGELDDLPE QAFYLVGNIN EALTKAASMK