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ATPF_SOLLC
ID   ATPF_SOLLC              Reviewed;         184 AA.
AC   Q2MIB4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
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   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. LA3023;
RX   PubMed=16575560; DOI=10.1007/s00122-006-0254-x;
RA   Daniell H., Lee S.-B., Grevich J., Saski C., Quesada-Vargas T., Guda C.,
RA   Tomkins J., Jansen R.K.;
RT   "Complete chloroplast genome sequences of Solanum bulbocastanum, Solanum
RT   lycopersicum and comparative analyses with other Solanaceae genomes.";
RL   Theor. Appl. Genet. 112:1503-1518(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. IPA-6;
RX   PubMed=16830097; DOI=10.1007/s00239-005-0254-5;
RA   Kahlau S., Aspinall S., Gray J.C., Bock R.;
RT   "Sequence of the tomato chloroplast DNA and evolutionary comparison of
RT   solanaceous plastid genomes.";
RL   J. Mol. Evol. 63:194-207(2006).
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; DQ347959; ABC56286.1; -; Genomic_DNA.
DR   EMBL; AM087200; CAJ32379.1; -; Genomic_DNA.
DR   RefSeq; AP_004914.1; AC_000188.1.
DR   RefSeq; YP_008563074.1; NC_007898.3.
DR   AlphaFoldDB; Q2MIB4; -.
DR   SMR; Q2MIB4; -.
DR   STRING; 4081.Solyc12g027720.1.1; -.
DR   PaxDb; Q2MIB4; -.
DR   PRIDE; Q2MIB4; -.
DR   GeneID; 3950472; -.
DR   KEGG; sly:3950472; -.
DR   InParanoid; Q2MIB4; -.
DR   OrthoDB; 1333093at2759; -.
DR   Proteomes; UP000004994; Chloroplast.
DR   ExpressionAtlas; Q2MIB4; baseline.
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; Reference proteome;
KW   Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..184
FT                   /note="ATP synthase subunit b, chloroplastic"
FT                   /id="PRO_0000277422"
FT   TRANSMEM        27..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   184 AA;  20872 MW;  196E6F5B69DE846F CRC64;
     MKNVTDSFVS LGHWPSAGSF GFNTDILATN PINLSVVLGV LIFFGKGVLS DLLDNRKQRI
     LNTIRNSEEL RGGAIEQLEK ARSRLRKVET EAEQFRVNGY SEIEREKLNL INSTYKTLEQ
     LENYKNETIQ FEQQRAINQV RQRVFQQALR GALGTLNSCL NNELHLRTIS ANIGMLGTMK
     EITD
 
 
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