ATPB_OCHNE
ID ATPB_OCHNE Reviewed; 475 AA.
AC Q40612;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=atpD {ECO:0000255|HAMAP-Rule:MF_01347};
OS Ochrosphaera neapolitana.
OG Plastid; Chloroplast.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Coccolithales;
OC Hymenomonadaceae; Ochrosphaera.
OX NCBI_TaxID=35137;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CCMP593 / OCHRO / Plymouth163;
RA Saez A.G., Engel H., Medlin L.K., Huss V.A.R.;
RT "Plastid genome size and heterogeneous base composition of nuclear DNA from
RT Ochrosphaera neapolitana (Prymnesiophyta).";
RL Phycologia 40:147-152(2001).
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; X99079; CAA67541.1; -; Genomic_DNA.
DR AlphaFoldDB; Q40612; -.
DR SMR; Q40612; -.
DR PRIDE; Q40612; -.
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_0000254503"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 475 AA; 50969 MW; D297D5719E64B47A CRC64;
MVDVASKTGI ISQIIGPVVD VEFSSGDLPK VYNAIVIDAG DKKVTCEVQQ LLGNNKVRAV
SMTSTDGLKR GASVLDTGSP ITVPVGVPTL GRIFNVLGEP VDELGPCNAE SGLPIHRPAP
SFTELETKPS VFETGIKVVD LLAPYKRGGK IGLFGGAGVG KTVLIMELIN NIAKAHGGVS
VFGGVGERTR EGNDLYAEMK ESKVIDEDKL ENSKVALVYG QMNEPPGARM RVGLTALTMA
EYFRDVNKQD VLLFIDHIFR FVQAGSEVSA LLGSMPSAVG YQPTLATEMG VLQERITSTN
EGSITSIQAV YVPADDLTDP APATTFAHLD ATTVLSRGLA SKGIYPAVDP LDSTSTMLQP
EIVGTEHYAT AQRIKETLQR YKELQDIIAI LGLDELSEDD RLTVSRARKV ERFLSQPFFV
AEVFTGSPGK YVSLNDSIDG FNRLLNGEFD DLPEQSFYLV GDINEAIAKA AKLKG
