ID   ATPF_ADICA              Reviewed;         184 AA.
AC   Q85FN3;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   25-MAY-2022, entry version 70.
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   Adiantum capillus-veneris (Maidenhair fern).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC   Vittarioideae; Adiantum.
OX   NCBI_TaxID=13818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12755170; DOI=10.1093/dnares/10.2.59;
RA   Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M.;
RT   "Complete nucleotide sequence of the chloroplast genome from a
RT   leptosporangiate fern, Adiantum capillus-veneris L.";
RL   DNA Res. 10:59-65(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RC   TISSUE=Frond;
RX   PubMed=15363849; DOI=10.1016/j.gene.2004.06.018;
RA   Wolf P.G., Rowe C.A., Hasebe M.;
RT   "High levels of RNA editing in a vascular plant chloroplast genome:
RT   analysis of transcripts from the fern Adiantum capillus-veneris.";
RL   Gene 339:89-97(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   -!- RNA EDITING: Modified_positions=1 {ECO:0000269|PubMed:15363849};
CC       Note=The initiator methionine is created by RNA editing.;
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; AY178864; AAP29378.2; -; Genomic_DNA.
DR   RefSeq; NP_848046.2; NC_004766.1.
DR   AlphaFoldDB; Q85FN3; -.
DR   SMR; Q85FN3; -.
DR   GeneID; 807366; -.
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_0000082400"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   184 AA;  21407 MW;  64C5AA60774B93A0 CRC64;
     MRSLSEIIAP SSYWTLAGTI GLNTNIFEIN LINLILVLGI LFYYGKGVLI NLLENRERTI
     LNTIQDAEER HKEATEKLQR ARLRLQQAEM KADEIRIIGL TKMDRERRDL VDAADNDLRE
     LEESKNYAIR FEKQRAIEQV RQQVSRLASE RAFESLNGRL TNEFQLRMID YHIGLLRAMA
     NKST