ID   ATPB_CHAMQ              Reviewed;          20 AA.
AC   C0HLQ4;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=ATP synthase subunit beta, chloroplastic {ECO:0000305};
DE            EC=7.1.2.2 {ECO:0000305};
DE   AltName: Full=ATP synthase F1 subunit beta {ECO:0000305};
DE   AltName: Full=F-ATPase subunit beta {ECO:0000305};
DE   Flags: Fragment;
OS   Chattonella marina var. antiqua (Red tide flagellate) (Chattonella
OS   antiqua).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Raphidophyceae; Chattonellales;
OC   Chattonellaceae; Chattonella.
OX   NCBI_TaxID=859642;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   STRAIN=NIES-1 {ECO:0000303|PubMed:23291769};
RX   PubMed=23291769; DOI=10.1271/bbb.120543;
RA   Qiu X., Shimasaki Y., Tsuyama M., Yamada T., Kuwahara R., Kawaguchi M.,
RA   Honda M., Gunjikake H., Tasmin R., Shimizu M., Sato Y., Kato-Unoki Y.,
RA   Nakashima T., Matsubara T., Yamasaki Y., Ichinose H., Wariishi H.,
RA   Honjo T., Oshima Y.;
RT   "Growth-phase dependent variation in photosynthetic activity and cellular
RT   protein expression profile in the harmful raphidophyte Chattonella
RT   antiqua.";
RL   Biosci. Biotechnol. Biochem. 77:46-52(2013).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND INDUCTION.
RC   STRAIN=NIES-1 {ECO:0000303|Ref.2};
RX   DOI=10.1016/j.jembe.2020.151361;
RA   Qiu X., Mukai K., Shimasaki Y., Wu M., Chen C., Lu Y., Ichinose H.,
RA   Nakashima T., Kato-Unoki Y., Oshima Y.;
RT   "Diurnal variations in expression of photosynthesis-related proteins in the
RT   harmful Raphidophyceae Chattonella marina var. antiqua.";
RL   J. Exp. Mar. Biol. Ecol. 527:0-0(2020).
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:0000305}.
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:0000305};
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:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Expression shows a diurnal pattern of oscillation across the
CC       24-hour light-dark, with increased levels during the light period (at
CC       protein level). {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; C0HLQ4; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   ATP synthesis; Chloroplast; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Plastid; Thylakoid;
KW   Translocase; Transport.
FT   CHAIN           1..>20
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000450203"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         20
FT                   /evidence="ECO:0000303|PubMed:23291769"
SQ   SEQUENCE   20 AA;  2196 MW;  3B79CE29AC7ADA0B CRC64;
     METTNESLGY TDQIIGPVLD