ATPF_ORYSJ
ID ATPF_ORYSJ Reviewed; 183 AA.
AC P0C2Z0; P12087; Q6QXV1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=ATP synthase subunit b, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398};
GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; ORFNames=Nip045;
OS Oryza sativa subsp. japonica (Rice).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=2770692; DOI=10.1007/bf02464880;
RA Hiratsuka J., Shimada H., Whittier R., Ishibashi T., Sakamoto M., Mori M.,
RA Kondo C., Honji Y., Sun C.-R., Meng B.-Y., Li Y.-Q., Kanno A.,
RA Nishizawa Y., Hirai A., Shinozaki K., Sugiura M.;
RT "The complete sequence of the rice (Oryza sativa) chloroplast genome:
RT intermolecular recombination between distinct tRNA genes accounts for a
RT major plastid DNA inversion during the evolution of the cereals.";
RL Mol. Gen. Genet. 217:185-194(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15122023; DOI=10.1104/pp.103.031245;
RA Tang J., Xia H., Cao M., Zhang X., Zeng W., Hu S., Tong W., Wang J.,
RA Wang J., Yu J., Yang H., Zhu L.;
RT "A comparison of rice chloroplast genomes.";
RL Plant Physiol. 135:412-420(2004).
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main
CC subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC form an alternating ring which encloses part of the gamma chain. F(1)
CC is attached to F(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta, b and b'
CC chains. {ECO:0000255|HAMAP-Rule:MF_01398}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01398}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01398}.
CC -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as
CC CF(1)CF(0).
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS46117.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X15901; CAA33992.1; -; Genomic_DNA.
DR EMBL; AY522330; AAS46117.1; ALT_SEQ; Genomic_DNA.
DR PIR; JQ0219; LWRZ1.
DR RefSeq; NP_039379.1; NC_001320.1.
DR AlphaFoldDB; P0C2Z0; -.
DR SMR; P0C2Z0; -.
DR STRING; 39947.P0C2Z0; -.
DR PaxDb; P0C2Z0; -.
DR PRIDE; P0C2Z0; -.
DR GeneID; 3131391; -.
DR KEGG; osa:3131391; -.
DR InParanoid; P0C2Z0; -.
DR OrthoDB; 1333093at2759; -.
DR Proteomes; UP000059680; Chloroplast.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; IC:Gramene.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); 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-UniRule.
DR HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR Pfam; PF00430; ATP-synt_B; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; CF(0); Chloroplast; Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Plastid; Reference proteome;
KW Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..183
FT /note="ATP synthase subunit b, chloroplastic"
FT /id="PRO_0000288517"
FT TRANSMEM 27..49
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT CONFLICT 181..183
FT /note="Missing (in Ref. 1; CAA33992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 183 AA; 20956 MW; 0F9F1C3C9E35A695 CRC64;
MKNVTHSFVF LAHWPSAGSF GLNTDILATN LINLTVVVGV LIYFGKGVLK DLLDNRKQRI
LSTIRNSEEL RRGTIEQLEK ARIRLQKVEL EADEYRMNGY SEIEREKANL INATSISLEQ
LEKSKNETLY FEKQRAMNQV RQRVFQQAVQ GALGTLNSCL NTELHFRTIR ANISILGAME
WKS
