ID   ATPF_TOBAC              Reviewed;         184 AA.
AC   P06290;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 3.
DT   25-MAY-2022, entry version 112.
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   Nicotiana tabacum (Common tobacco).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Bright Yellow 4;
RX   PubMed=16453699; DOI=10.1002/j.1460-2075.1986.tb04464.x;
RA   Shinozaki K., Ohme M., Tanaka M., Wakasugi T., Hayashida N.,
RA   Matsubayashi T., Zaita N., Chunwongse J., Obokata J.,
RA   Yamaguchi-Shinozaki K., Ohto C., Torazawa K., Meng B.-Y., Sugita M.,
RA   Deno H., Kamogashira T., Yamada K., Kusuda J., Takaiwa F., Kato A.,
RA   Tohdoh N., Shimada H., Sugiura M.;
RT   "The complete nucleotide sequence of the tobacco chloroplast genome: its
RT   gene organization and expression.";
RL   EMBO J. 5:2043-2049(1986).
RN   [2]
RP   SEQUENCE REVISION.
RA   Yukawa M.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   RNA EDITING.
RX   PubMed=8605316; DOI=10.1007/bf00049342;
RA   Hirose T., Fan H., Suzuki J.Y., Wakasugi T., Tsudzuki T., Kossel H.,
RA   Sugiura M.;
RT   "Occurrence of silent RNA editing in chloroplasts: its species specificity
RT   and the influence of environmental and developmental conditions.";
RL   Plant Mol. Biol. 30:667-672(1996).
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   -!- RNA EDITING: Modified_positions=31 {ECO:0000269|PubMed:8605316};
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z00044; CAA77342.2; ALT_SEQ; Genomic_DNA.
DR   PIR; A01060; LWNT1.
DR   RefSeq; NP_054482.2; NC_001879.2.
DR   AlphaFoldDB; P06290; -.
DR   SMR; P06290; -.
DR   GeneID; 800473; -.
DR   KEGG; nta:800473; -.
DR   OrthoDB; 1333093at2759; -.
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   2: Evidence at transcript level;
KW   ATP synthesis; ATP-binding; CF(0); Chloroplast; Hydrogen ion transport;
KW   Ion transport; Membrane; Nucleotide-binding; Plastid; RNA editing;
KW   Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..184
FT                   /note="ATP synthase subunit b, chloroplastic"
FT                   /id="PRO_0000082424"
FT   TRANSMEM        27..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   184 AA;  20874 MW;  A827EE9ABD128305 CRC64;
     MKNVTDSFVS LGHWPSAGSF GFNTDILATN LINLSVVLGV LIFFGKGVLS DLLDNRKQRI
     LNTIRNSEEL RGGAIEQLEK ARSRLRKVES EAEQFRVNGY SEIEREKLNL INSTYKTLEQ
     LENYKNETIQ FEQQRAINQV RQRVFQQALR GALGTLNSCL NNELHLRTIS ANIGMLGTMK
     EITD