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ATPB_THAPS
ID   ATPB_THAPS              Reviewed;         474 AA.
AC   A0T0R6;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 / NEPCC58 / CCAP 1085/12;
RX   PubMed=17252281; DOI=10.1007/s00438-006-0199-4;
RA   Oudot-Le Secq M.-P., Grimwood J., Shapiro H., Armbrust E.V., Bowler C.,
RA   Green B.R.;
RT   "Chloroplast genomes of the diatoms Phaeodactylum tricornutum and
RT   Thalassiosira pseudonana: comparison with other plastid genomes of the red
RT   lineage.";
RL   Mol. Genet. Genomics 277:427-439(2007).
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; EF067921; ABK20751.1; -; Genomic_DNA.
DR   RefSeq; YP_874528.1; NC_008589.1.
DR   AlphaFoldDB; A0T0R6; -.
DR   SMR; A0T0R6; -.
DR   STRING; 35128.Thapsdraft1563; -.
DR   PRIDE; A0T0R6; -.
DR   GeneID; 4524734; -.
DR   eggNOG; KOG1350; Eukaryota.
DR   InParanoid; A0T0R6; -.
DR   OMA; IDVYFPE; -.
DR   Proteomes; UP000001449; Chloroplast.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
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   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
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..474
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000275190"
FT   BINDING         155..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   474 AA;  51142 MW;  530DA3525DBCC107 CRC64;
     MVETTNKGYV CQIIGPVLDI EFPGGKLPPI YSAIKIETAD GIGNIVEVQQ LLGDNKVRAV
     SMRSTDGLKR GVEAVDLGAP ITVPVGVPTL GRIFNVIGEP VDEQGDVVVD QTLPIHRDAP
     AFTELETKPS IFETGIKVVD LLAPYRRGGK IGLFGGAGVG KTVLIMELIN NIAKAHGGVS
     VFGGVGERTR EGNDLYEEMK ESGVINSSNF AESKVALVYG QMNEPPGARM RVGLTALTMA
     EYFRDVNKQD VLLFIDNIFR FTQAGSEVSA LLGRMPSAVG YQPTLATEMG ALQERITSTT
     QGSITSIQAV YVPADDLTDP APATTFAHLD ATTVLSRNLA AKGIYPAVDP LDSTSTMLQP
     GIVSEVHYET AETVKETLQR YKELQDIIAI LGIDELSEED RLVVARARKV ERFLSQPFFV
     AEIFTGSPGK YVSLEETIKG FTMILNGELD DLPEQSFYLV GNIDEAIAKA ETLK
 
 
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