ID   ATPF_CUSRE              Reviewed;         184 AA.
AC   A7M952;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=ATP synthase subunit b, plastid {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   Cuscuta reflexa (Southern Asian dodder).
OG   Plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC   Cuscuta subgen. Monogynella.
OX   NCBI_TaxID=4129;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX   PubMed=17714582; DOI=10.1186/1471-2229-7-45;
RA   Funk H.T., Berg S., Krupinska K., Maier U.-G., Krause K.;
RT   "Complete DNA sequences of the plastid genomes of two parasitic flowering
RT   plant species, Cuscuta reflexa and Cuscuta gronovii.";
RL   BMC Plant Biol. 7:45-45(2007).
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 membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_01398}.
CC   -!- RNA EDITING: Modified_positions=31 {ECO:0000269|PubMed:17714582};
CC   -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01398}.
CC   -!- CAUTION: Young tissue from this organism is photosynthetic and contains
CC       some thylakoids, although the photosynthetic activity does not exceed
CC       the light compensation point. {ECO:0000305}.
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DR   EMBL; AM711640; CAM98380.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; YP_001430094.1; NC_009766.1.
DR   AlphaFoldDB; A7M952; -.
DR   SMR; A7M952; -.
DR   GeneID; 5536596; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042170; C:plastid membrane; IEA:UniProtKB-SubCell.
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:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
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); Hydrogen ion transport; Ion transport;
KW   Membrane; Nucleotide-binding; Plastid; RNA editing; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..184
FT                   /note="ATP synthase subunit b, plastid"
FT                   /id="PRO_0000308479"
FT   TRANSMEM        27..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   184 AA;  20900 MW;  2FEC059A74260851 CRC64;
     MKNVTDSFLS LGHWSSAGSF GLNTDILATN LINLSVVLGV LIFFGKGVLS DLLDNRKRRI
     LKTIQNSEEL GVGAVEKLEK ARARLRKVKT EAEQFLVNGY FDIEQEKLNL IKSTYNTLEQ
     LENDKNENLR FEQQRVIYQV RQRFFQKALQ RAIGTLNGCL NNELHLRTIS ANIGMLGTIK
     EITD