ATPB_GALSU
ID ATPB_GALSU Reviewed; 476 AA.
AC Q08807;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 123.
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 Galdieria sulphuraria (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Galdieria.
OX NCBI_TaxID=130081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=14-1-1 / Isolate 107.79/Goettingen;
RX PubMed=8219057; DOI=10.1007/bf00021420;
RA Kostrzewa M., Zetsche K.;
RT "Organization of plastid-encoded ATPase genes and flanking regions
RT including homologues of infB and tsf in the thermophilic red alga Galdieria
RT sulphuraria.";
RL Plant Mol. Biol. 23:67-76(1993).
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; X66698; CAA47241.1; -; Genomic_DNA.
DR PIR; S36412; S36412.
DR AlphaFoldDB; Q08807; -.
DR SMR; Q08807; -.
DR STRING; 130081.XP_005705031.1; -.
DR eggNOG; KOG1350; Eukaryota.
DR eggNOG; KOG1758; Eukaryota.
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..476
FT /note="ATP synthase subunit beta, chloroplastic"
FT /id="PRO_0000144514"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 476 AA; 51967 MW; A30500E1062213AC CRC64;
MSTIAQNKGY ISQIIGPVID IEFPNGTLPK IYNAISIKHK NKTITCEVQQ LLGDNRVRTV
AMNSTEGLQR GIEAIDTGSA ITVPVGKCTL GRIFNVLGEP VDELGAISTD RKLPIHRASP
LFTQLETKPS IFETGIKVID LLAPYKRGGK IGLFGGAGVG KTVLIMELIN NIAKSHGGVS
VFGGVGERTR EGNDLYVEMK ESKVINEKNL EESKVALVYG QMNEPPGARM RVGLTALTMA
EYFRDNNKQD VLLFIDNIFR FVQAGSEVSA LLGRMPSAVG YQPTLATEMG ALQERITSTK
EGSITSIQAV YVPADDLTDP APATTFAHLD ATTVLSRGLA SKGIYPAVDP LDSTSTMLQP
QIVGDEHYVT AQRVKENLQR YKELQDIIAI LGLDELSEED RLTVARARKI ERFLSQPFFV
AEVFTGSPGK YVSLKESIDG FKMILNGELD DLPEQAFYLV GNIQEAIKKA DELKDK
