ATPB_BLEOC
ID ATPB_BLEOC Reviewed; 395 AA.
AC O03066;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 109.
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};
DE Flags: Fragment;
GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_01347};
OS Blechnum occidentale (Hammock fern).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Aspleniineae; Blechnaceae;
OC Blechnoideae; Blechnum.
OX NCBI_TaxID=32073;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO N-TERMINUS AND
RP 238.
RA Wolf P.G., Su P.-H.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-372.
RC TISSUE=Frond;
RA Wolf P.G.;
RT "Evaluation of atpB nucleotide sequences for phylogenetic studies of ferns
RT and other pteridophytes.";
RL Am. J. Bot. 84:1429-1440(1997).
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; U93838; AAB51746.2; -; Genomic_DNA.
DR AlphaFoldDB; O03066; -.
DR SMR; O03066; -.
DR PRIDE; O03066; -.
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-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
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; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
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 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..395
FT /note="ATP synthase subunit beta, chloroplastic"
FT /id="PRO_0000144500"
FT BINDING 72..79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
FT NON_TER 1
SQ SEQUENCE 395 AA; 42418 MW; 5EF7BBCA549DB53F CRC64;
PVGETTLGRI SNVLGEPVDN LGPVQSSTTF PIHRSAPAFT QLDTKLSIFE TGIKVVDLSA
PYRRGGKIGL FGGAGVGKTV LITESINNIA KAHGGVSVSG GVGERTREGN DLYMEMKESK
VINEQNISES KVALVYGQMN EPPGARMRVG STASTMAEYF RDVNKQDVPP FIDNIFRFVQ
AGSEVSALLG RMPSAVGYQP TLGTEMGSLQ ERITSTKEGS ITSIQAVYVP ADDLTDPAPA
TTSAHLDATT VLSRGLAAKG IYPAVDPLDS TSTMLQPWIA GEEHYDTAQG VKQTLQRYKE
LQDIIAIPGL DELSEEDRLT VARARKIERF LSQPFFVAEV FTGSPGKYVS LSETIKGFQM
ILPGELDNLP EQAFYLVGNI DEATAKAASL QAEVQ