ATPB_TRICV
ID ATPB_TRICV Reviewed; 475 AA.
AC P49647;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 Trieres chinensis (Marine centric diatom) (Odontella sinensis).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae;
OC Biddulphiophycidae; Eupodiscales; Parodontellaceae; Trieres.
OX NCBI_TaxID=1514140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kroth-Pancic P., Freier U., Strotmann H., Kowallik K.V.;
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kowallik K.V., Stoebe B., Schaffran I., Kroth-Pancic P., Freier U.;
RT "The chloroplast genome of a chlorophyll a+c-containing alga, Odontella
RT sinensis.";
RL Plant Mol. Biol. Rep. 13:336-342(1995).
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; X72497; CAA51161.1; -; Genomic_DNA.
DR EMBL; Z67753; CAA91739.1; -; Genomic_DNA.
DR PIR; S78366; S78366.
DR AlphaFoldDB; P49647; -.
DR SMR; P49647; -.
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..475
FT /note="ATP synthase subunit beta, chloroplastic"
FT /id="PRO_0000144534"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 475 AA; 51509 MW; 5BDA89DAA9D4DA2C CRC64;
MVKTNINKGY VNQIIGPVLD IEFPSGTLPP IYSALKIETE DGIGTVVEVQ QLLGDNKVRA
VSMRSTDGLK RGVEARDLGG PISVPVGIST LGRIFNVIGE PVDEQGDVSY DETLPIHREA
PAFTELETKP SIFETGIKVV DLLAPYRRGG KIGLFGGAGV GKTVLIMELI NNIAKAHGGV
SVFGGVGERT REGNDLYEEM KESGVINENN FKESKVALVY GQMNEPPGAR MRVGLTALTM
AEYFRDVNKQ DVLLFIDNIF RFTQAGSEVS ALLGRMPSAV GYQPTLATEM GALQERITST
TQGSITSIQA VYVPADDLTD PAPATTFAHL DATTVLSRNL AAKGIYPAVD PLDSTSTMLQ
PGIVSGEHYE IAETVKETLQ RYKELQDIIA ILGIDELSEE DRLTVARARK VERFLSQPFF
VAEIFTGSPG KYVSLEETIK GFTMVLKGEL DELPEQAFYL VGNIDEAIAK AETLK
