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ATPF_WHEAT
ID   ATPF_WHEAT              Reviewed;         183 AA.
AC   P06528;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 108.
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};
OS   Triticum aestivum (Wheat).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16453616; DOI=10.1002/j.1460-2075.1985.tb03790.x;
RA   Bird C.R., Koller B., Auffret A.D., Huttly A.K., Howe C.J., Dyer T.A.,
RA   Gray J.C.;
RT   "The wheat chloroplast gene for CF-0 subunit I of ATP synthase contains a
RT   large intron.";
RL   EMBO J. 4:1381-1388(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring;
RA   Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T.,
RA   Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., Gojobori T.,
RA   Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., Tsunewaki K.;
RT   "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: complete
RT   sequence and contig clones.";
RL   Plant Mol. Biol. Rep. 18:243-253(2000).
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}.
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DR   EMBL; X02595; CAA26438.1; -; Genomic_DNA.
DR   EMBL; AB042240; BAB47030.1; -; Genomic_DNA.
DR   PIR; A22721; PWWT1.
DR   RefSeq; NP_114255.1; NC_002762.1.
DR   AlphaFoldDB; P06528; -.
DR   SMR; P06528; -.
DR   STRING; 4565.EPlTAEP00000010028; -.
DR   PRIDE; P06528; -.
DR   GeneID; 803099; -.
DR   KEGG; taes:803099; -.
DR   eggNOG; ENOG502S22I; Eukaryota.
DR   Proteomes; UP000019116; 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: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_0000082425"
FT   TRANSMEM        27..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   183 AA;  20977 MW;  0E3E4E5041520E36 CRC64;
     MKNVTHSFVF LAHWPSAGSF GLNTDILATN LINLTVVVGV LIFFGKGVLK DLLDNRKQRI
     LSTIRNSEEL RRGTIEQLEK ARIRLQKVEL EADEYRMNGY SEIEREKANL INATSISLEQ
     LEKSKNETLY FEKQRAMNQV RQRVFQQAVQ GALGTLNSCL NTELHFRTIR ANIGILGSLE
     WKR
 
 
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