ID   ATPF2_PAUCH             Reviewed;         156 AA.
AC   B1X3Y3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=ATP synthase subunit b', organellar chromatophore {ECO:0000255|HAMAP-Rule:MF_01399};
DE   AltName: Full=ATP synthase F(0) sector subunit b' {ECO:0000255|HAMAP-Rule:MF_01399};
DE   AltName: Full=ATPase subunit II {ECO:0000255|HAMAP-Rule:MF_01399};
GN   Name=atpF2 {ECO:0000255|HAMAP-Rule:MF_01399};
GN   Synonyms=atpG {ECO:0000255|HAMAP-Rule:MF_01399};
GN   OrderedLocusNames=PCC_0202;
OS   Paulinella chromatophora.
OG   Plastid; Organellar chromatophore.
OC   Eukaryota; Sar; Rhizaria; Imbricatea; Silicofilosea; Euglyphida;
OC   Paulinellidae; Paulinella.
OX   NCBI_TaxID=39717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA   Nowack E.C.M., Melkonian M., Gloeckner G.;
RT   "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT   photosynthesis by eukaryotes.";
RL   Curr. Biol. 18:410-418(2008).
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_01399}.
CC   -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC       peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged
CC       and duplicated form of b found in plants and photosynthetic bacteria.
CC       {ECO:0000255|HAMAP-Rule:MF_01399}.
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_01399}.
CC   -!- SUBCELLULAR LOCATION: Plastid, organellar chromatophore thylakoid
CC       membrane {ECO:0000250}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_01399}.
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_01399}.
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; CP000815; ACB42652.1; -; Genomic_DNA.
DR   RefSeq; YP_002048862.1; NC_011087.1.
DR   AlphaFoldDB; B1X3Y3; -.
DR   SMR; B1X3Y3; -.
DR   GeneID; 6481242; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0070118; C:organellar chromatophore thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); 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   HAMAP; MF_01399; ATP_synth_bprime; 1.
DR   InterPro; IPR034679; ATP_synth_b.
DR   InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR   InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   Pfam; PF00430; ATP-synt_B; 1.
DR   SUPFAM; SSF81573; SSF81573; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Organellar chromatophore; Plastid; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..156
FT                   /note="ATP synthase subunit b', organellar chromatophore"
FT                   /id="PRO_0000369058"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01399"
SQ   SEQUENCE   156 AA;  17512 MW;  9F99D9D6EFD431DD CRC64;
     MTSWLLLAEA GVPEGGLFDL DATLPLMAIQ VVFLTFILNA IFFRPIGRTV EERENYVASS
     RADAKQKLAQ VERLEANLTE QLRGARKQSQ TVIAEAEEEV NRLYQEALRM AQAEANNIRE
     SSRREIEIQK AAAIKSLQGD VDRLSNLIVD RLLASR