ID   ATPB_CYAM1              Reviewed;         467 AA.
AC   Q85FT2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
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   Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC   Cyanidioschyzon.
OX   NCBI_TaxID=280699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3377 / 10D;
RX   PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA   Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA   Shin-i T., Kohara Y., Kuroiwa T.;
RT   "Complete sequence and analysis of the plastid genome of the unicellular
RT   red alga Cyanidioschyzon merolae.";
RL   DNA Res. 10:67-77(2003).
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; AB002583; BAC76263.1; -; Genomic_DNA.
DR   RefSeq; NP_849101.1; NC_004799.1.
DR   AlphaFoldDB; Q85FT2; -.
DR   SMR; Q85FT2; -.
DR   STRING; 45157.CMV196CT; -.
DR   EnsemblPlants; CMV196CT; CMV196CT; CMV196C.
DR   GeneID; 844866; -.
DR   Gramene; CMV196CT; CMV196CT; CMV196C.
DR   KEGG; cme:CymeCp169; -.
DR   eggNOG; KOG1350; Eukaryota.
DR   HOGENOM; CLU_022398_0_2_1; -.
DR   Proteomes; UP000007014; Chloroplast.
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:0003729; F:mRNA binding; IEA:EnsemblPlants.
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:0050832; P:defense response to fungus; IEA:EnsemblPlants.
DR   GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
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..467
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000254470"
FT   BINDING         149..156
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   467 AA;  50414 MW;  D161C0F07D42A44C CRC64;
     MSGKVVQIIG PVLDIEFPSG QLPKLLNAIV VRDGEKSVTC EVQQLLGDNR VRAIAMSSTD
     GLRRGIQAED TGAPISVPVG KVTLGRIFNV LGDCVDNLGT VTRQAVQPIH KQAPSFVQLE
     TKPSVFETGI KVVDLLAPYR RGGKIGLFGG AGVGKTVLIM ELINNIAKAH GGVSVFAGVG
     ERTREGNDLY EEMKASGVIQ SQNLSESKVA LCYGQMNEPP GARMRVGLTA LTMAEHFRDI
     NKQDVLLFID NIFRFVQAGS EVSALLGRMP SAVGYQPTLA TEMGALQERI TSTVDGSITS
     IQAVYVPADD LTDPAPATTF AHLDATTVLS RGLAAKGIYP AVDPLDSTST MLQPNIVGEA
     HYQTASRVKQ TLQRYKELQD IIAILGLDEL SEEDRLLVAR ARKIERFLSQ PFFVAEVFTG
     SPGKYVSLEE SIKGFKMILD GELDDLPEQA FYLVGNIEEA IQKAQKL