ID   ATPB_TUPAK              Reviewed;         481 AA.
AC   Q3ZJ68;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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   Tupiella akineta (Green alga) (Pseudendoclonium akinetum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; OUU clade;
OC   Ulotrichales; Tupiellaceae; Tupiella.
OX   NCBI_TaxID=160070;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX 1912;
RX   PubMed=15930151; DOI=10.1093/molbev/msi182;
RA   Pombert J.-F., Otis C., Lemieux C., Turmel M.;
RT   "The chloroplast genome sequence of the green alga Pseudendoclonium
RT   akinetum (Ulvophyceae) reveals unusual structural features and new insights
RT   into the branching order of chlorophyte lineages.";
RL   Mol. Biol. Evol. 22:1903-1918(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; AY835431; AAV80623.1; -; Genomic_DNA.
DR   RefSeq; YP_636199.1; NC_008114.1.
DR   AlphaFoldDB; Q3ZJ68; -.
DR   SMR; Q3ZJ68; -.
DR   GeneID; 4108803; -.
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_0000254517"
FT   BINDING         163..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   481 AA;  51735 MW;  8C19C2DBBEF1306E CRC64;
     MVLSIQTNKN VGSITQIIGP VIDAAFAPGQ LPNIYNALVI KGTNQAGQEV AVTCEVQQLL
     GDHCVRAVAM NATDGLMRGM NIVDTGKPLT VPVGKVTLGR IFNVLGEPVD GLEAVDSKES
     LPIHRKAPAF VDLDTKLAIF ETGIKVVDLL APYRRGGKIG LFGGAGVGKT VLIMELINNI
     AKAHGGVSVF GGVGERTREG NDLYMEMKES GVIQEKNMSA SKVALVYGQM NEPPGARMRV
     GLTALTMAEY FRDINKQDVL LFIDNIFRFV QAGSEVSALL GRMPSAVGYQ PTLATEMGGL
     QERITSTKDG SITSIQAVYV PADDLTDPAP ATTFAHLDAT TVLSRGLASK GIYPAVDPLD
     STSTMLQPWI VGEEHYSCAQ NVKETLQRYK ELQDIIAILG LDELSEEDRK VVARARKIER
     FLSQPFFVAE VFTGSPGKYV SLKETIQGFN KILTGELDDL PEQAFYLVGT LDEAVAKAAT
     L