ID   ATPB_ARATH              Reviewed;         498 AA.
AC   P19366;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   24-JAN-2024, entry version 187.
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};
GN   OrderedLocusNames=AtCg00480;
OS   Arabidopsis thaliana (Mouse-ear cress).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10574454; DOI=10.1093/dnares/6.5.283;
RA   Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT   "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL   DNA Res. 6:283-290(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 486-498.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=2904134; DOI=10.1093/nar/16.21.10372;
RA   Chen H.-C., Wintz H., Weil J.-H., Pillay D.T.N.;
RT   "Nucleotide sequence of chloroplast CF1-ATPase epsilon-subunit and
RT   elongator tRNAMet genes from Arabidopsis thaliana.";
RL   Nucleic Acids Res. 16:10372-10372(1988).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [4]
RP   INTERACTION WITH RBCX1.
RX   PubMed=21922322; DOI=10.1007/s11103-011-9823-8;
RA   Kolesinski P., Piechota J., Szczepaniak A.;
RT   "Initial characteristics of RbcX proteins from Arabidopsis thaliana.";
RL   Plant Mol. Biol. 77:447-459(2011).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22092075; DOI=10.1021/pr200917t;
RA   Aryal U.K., Krochko J.E., Ross A.R.;
RT   "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT   polyethylene glycol fractionation, immobilized metal-ion affinity
RT   chromatography, two-dimensional gel electrophoresis and mass
RT   spectrometry.";
RL   J. Proteome Res. 11:425-437(2012).
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). Interacts with RBCX1
CC       (PubMed:21922322). {ECO:0000255|HAMAP-Rule:MF_01347,
CC       ECO:0000269|PubMed:21922322}.
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; AP000423; BAA84392.1; -; Genomic_DNA.
DR   EMBL; X12889; CAA31380.1; -; Genomic_DNA.
DR   PIR; S01904; S01904.
DR   RefSeq; NP_051066.1; NC_000932.1.
DR   AlphaFoldDB; P19366; -.
DR   SMR; P19366; -.
DR   BioGRID; 29961; 7.
DR   IntAct; P19366; 2.
DR   MINT; P19366; -.
DR   STRING; 3702.P19366; -.
DR   iPTMnet; P19366; -.
DR   MetOSite; P19366; -.
DR   PaxDb; 3702-ATCG00480-1; -.
DR   ProteomicsDB; 241075; -.
DR   EnsemblPlants; ATCG00480.1; ATCG00480.1; ATCG00480.
DR   GeneID; 844757; -.
DR   Gramene; ATCG00480.1; ATCG00480.1; ATCG00480.
DR   KEGG; ath:ArthCp029; -.
DR   Araport; ATCG00480; -.
DR   TAIR; ATCG00480; PB.
DR   eggNOG; KOG1350; Eukaryota.
DR   HOGENOM; CLU_022398_0_2_1; -.
DR   InParanoid; P19366; -.
DR   OMA; IDVYFPE; -.
DR   OrthoDB; 3420200at2759; -.
DR   BioCyc; ARA:ATCG00480-MONOMER; -.
DR   PRO; PR:P19366; -.
DR   Proteomes; UP000006548; Chloroplast Pltd.
DR   ExpressionAtlas; P19366; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009544; C:chloroplast ATP synthase complex; ISS:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR   GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0010287; C:plastoglobule; HDA:TAIR.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0010319; C:stromule; IDA:TAIR.
DR   GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR   GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
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:0008270; F:zinc ion binding; HDA:TAIR.
DR   GO; GO:0050832; P:defense response to fungus; IDA:TAIR.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR   CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR   CDD; cd01133; F1-ATPase_beta_CD; 1.
DR   Gene3D; 2.40.10.170; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR01039; atpD; 1.
DR   PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR   PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
DR   SWISS-2DPAGE; P19366; -.
DR   Genevisible; P19366; AT.
PE   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; CF(1); Chloroplast; Hydrogen ion transport;
KW   Ion transport; Membrane; Nucleotide-binding; Phosphoprotein; Plastid;
KW   Reference proteome; Thylakoid; Translocase; Transport.
FT   CHAIN           1..498
FT                   /note="ATP synthase subunit beta, chloroplastic"
FT                   /id="PRO_0000144496"
FT   BINDING         172..179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT   MOD_RES         6
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22092075"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   498 AA;  53934 MW;  174F4B075E7D57E3 CRC64;
     MRTNPTTSNP EVSIREKKNL GRIAQIIGPV LDVAFPPGKM PNIYNALVVK GRDTLGQEIN
     VTCEVQQLLG NNRVRAVAMS ATEGLKRGMD VVDMGNPLSV PVGGATLGRI FNVLGEPVDN
     LGPVDTRTTS PIHKSAPAFI ELDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV
     LIMELINNIA KAHGGVSVFG GVGERTREGN DLYMEMKESG VINEQNLAES KVALVYGQMN
     EPPGARMRVG LTALTMAEYF RDVNEQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP
     TLSTEMGTLQ ERITSTKKGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLAAKG
     IYPAVDPLDS TSTMLQPRIV GEEHYETAQQ VKQTLQRYKE LQDIIAILGL DELSEEDRLT
     VARARKIERF LSQPFFVAEV FTGSPGKYVG LAETIRGFNL ILSGEFDSLP EQAFYLVGNI
     DEATAKATNL EMESKLKK
//