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ATPB_GALSU
ID   ATPB_GALSU              Reviewed;         476 AA.
AC   Q08807;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 123.
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   Galdieria sulphuraria (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Galdieria.
OX   NCBI_TaxID=130081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=14-1-1 / Isolate 107.79/Goettingen;
RX   PubMed=8219057; DOI=10.1007/bf00021420;
RA   Kostrzewa M., Zetsche K.;
RT   "Organization of plastid-encoded ATPase genes and flanking regions
RT   including homologues of infB and tsf in the thermophilic red alga Galdieria
RT   sulphuraria.";
RL   Plant Mol. Biol. 23:67-76(1993).
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; X66698; CAA47241.1; -; Genomic_DNA.
DR   PIR; S36412; S36412.
DR   AlphaFoldDB; Q08807; -.
DR   SMR; Q08807; -.
DR   STRING; 130081.XP_005705031.1; -.
DR   eggNOG; KOG1350; Eukaryota.
DR   eggNOG; KOG1758; Eukaryota.
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..476
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000144514"
FT   BINDING         155..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   476 AA;  51967 MW;  A30500E1062213AC CRC64;
     MSTIAQNKGY ISQIIGPVID IEFPNGTLPK IYNAISIKHK NKTITCEVQQ LLGDNRVRTV
     AMNSTEGLQR GIEAIDTGSA ITVPVGKCTL GRIFNVLGEP VDELGAISTD RKLPIHRASP
     LFTQLETKPS IFETGIKVID LLAPYKRGGK IGLFGGAGVG KTVLIMELIN NIAKSHGGVS
     VFGGVGERTR EGNDLYVEMK ESKVINEKNL EESKVALVYG QMNEPPGARM RVGLTALTMA
     EYFRDNNKQD VLLFIDNIFR FVQAGSEVSA LLGRMPSAVG YQPTLATEMG ALQERITSTK
     EGSITSIQAV YVPADDLTDP APATTFAHLD ATTVLSRGLA SKGIYPAVDP LDSTSTMLQP
     QIVGDEHYVT AQRVKENLQR YKELQDIIAI LGLDELSEED RLTVARARKI ERFLSQPFFV
     AEVFTGSPGK YVSLKESIDG FKMILNGELD DLPEQAFYLV GNIQEAIKKA DELKDK
 
 
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