ATPB_HELAN
ID ATPB_HELAN Reviewed; 498 AA.
AC Q1KXV2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, 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 Helianthus annuus (Common sunflower).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HA383;
RA Timme R.E., Kuehl J.V., Boore J.L., Jansen R.K.;
RT "A comparison of the first two published chloroplast genomes in Asteraceae:
RT Lactuca and Helianthus.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; DQ383815; ABD47153.1; -; Genomic_DNA.
DR RefSeq; YP_588124.1; NC_007977.1.
DR AlphaFoldDB; Q1KXV2; -.
DR SMR; Q1KXV2; -.
DR PRIDE; Q1KXV2; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr02g0061551; CDS:HanXRQr2_Chr02g0061551.1; HanXRQr2_Chr02g0061551.
DR GeneID; 4055708; -.
DR Gramene; mRNA:HanXRQr2_Chr02g0061551; CDS:HanXRQr2_Chr02g0061551.1; HanXRQr2_Chr02g0061551.
DR KEGG; han:4055708; -.
DR PhylomeDB; Q1KXV2; -.
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..498
FT /note="ATP synthase subunit beta, chloroplastic"
FT /id="PRO_0000254480"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 498 AA; 53567 MW; 9C11D71802B74A73 CRC64;
MRMNPTTSSS GVATLDKKNL GRIAQIIGPV LDVAFPPGKM PNIYNALVVK GRDTVGQPIN
VTCEVQQLLG NNRVRAVAMS ATDGLTRGMD VIDTGAPLSV PVGGATLGRI FNVLGEPIDN
LGPVDNSTTF PIHRSAPAFI QLDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV
LIMELINNIA KAHGGVSVFG GVGERTREGN DLYMEMKESG VINEQNIAES KVALVYGQMN
EPPGARMRVG LTALTMAEYF RDVNEQDVLL FVDNIFRFVQ AGSEVSALLG RMPSAVGYQP
TLSTEMGSLQ ERITSTKEGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLAAKG
IYPAVDPLDS TSTMLQPRIV GDEHYETAQQ VKQTLQRYKE LQDIIAILGL DELSEEDRLT
VARARKIERF LSQPFFVAEV FTGSPGKYVG LAETIRGFQL ILSGELDGLP EQAFYLVGNI
DEATAKAMNL EMESNSKK
