ID   ATPF_OCHNE              Reviewed;         178 AA.
AC   Q40609;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 83.
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   Ochrosphaera neapolitana.
OG   Plastid; Chloroplast.
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Coccolithales;
OC   Hymenomonadaceae; Ochrosphaera.
OX   NCBI_TaxID=35137;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCMP593 / OCHRO / Plymouth163;
RA   Huss V.A.R., Tietze A.C., Julius C.;
RT   "Plastid genome size and heterogeneous base composition of nuclear DNA from
RT   Ochrosphaera neapolitana (Prymnesiophyta).";
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
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; X99078; CAA67538.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q40609; -.
DR   SMR; Q40609; -.
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; Thylakoid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..178
FT                   /note="ATP synthase subunit b, chloroplastic"
FT                   /id="PRO_0000082415"
FT   TRANSMEM        34..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   178 AA;  19657 MW;  5C4BC682938D805A CRC64;
     MHLFTQTLVR FSSLIADGGV SFNPDIFETN VVNLAILTGG IFYLGSNALS ESLVERQQKI
     LGAIQEAEER LEQATERLKE SKTQLEQAQL VIASIKEDAE TTAKQVKSAI LTEGKNEIER
     LTSAAKSQIV TIEAQVRKQI SDYVVSLALQ RVTLQLEGKL SDAAQQQILD RNISKLKD