ATPB_ARATH
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 03-AUG-2022, entry version 181.
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}; 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.ATCG00480.1; -.
DR iPTMnet; P19366; -.
DR MetOSite; P19366; -.
DR SWISS-2DPAGE; P19366; -.
DR PaxDb; P19366; -.
DR PRIDE; P19366; -.
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; locus:504954671; ATCG00480.
DR eggNOG; KOG1350; Eukaryota.
DR HOGENOM; CLU_022398_0_2_1; -.
DR InParanoid; P19366; -.
DR OMA; IDVYFPE; -.
DR OrthoDB; 495235at2759; -.
DR BioCyc; ARA:ATCG00480-MON; -.
DR PRO; PR:P19366; -.
DR Proteomes; UP000006548; Chloroplast.
DR ExpressionAtlas; P19366; baseline and differential.
DR Genevisible; P19366; AT.
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:0005753; C:mitochondrial proton-transporting ATP synthase complex; IBA:GO_Central.
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); IBA:GO_Central.
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: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:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
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 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
