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ATPF_ARATH
ID   ATPF_ARATH              Reviewed;         184 AA.
AC   P56759;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 132.
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}; OrderedLocusNames=AtCg00130;
OS   Arabidopsis thaliana (Mouse-ear cress).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10574454; DOI=10.1093/dnares/6.5.283;
RA   Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT   "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL   DNA Res. 6:283-290(1999).
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; AP000423; BAA84371.1; -; Genomic_DNA.
DR   RefSeq; NP_051045.1; NC_000932.1.
DR   AlphaFoldDB; P56759; -.
DR   SMR; P56759; -.
DR   BioGRID; 29983; 2.
DR   STRING; 3702.ATCG00130.1; -.
DR   iPTMnet; P56759; -.
DR   PaxDb; P56759; -.
DR   PRIDE; P56759; -.
DR   ProteomicsDB; 241091; -.
DR   EnsemblPlants; ATCG00130.1; ATCG00130.1; ATCG00130.
DR   GeneID; 844789; -.
DR   Gramene; ATCG00130.1; ATCG00130.1; ATCG00130.
DR   KEGG; ath:ArthCp008; -.
DR   Araport; ATCG00130; -.
DR   TAIR; locus:504954637; ATCG00130.
DR   eggNOG; ENOG502S22I; Eukaryota.
DR   HOGENOM; CLU_079215_8_0_1; -.
DR   InParanoid; P56759; -.
DR   OMA; QRTINQV; -.
DR   OrthoDB; 1333093at2759; -.
DR   BioCyc; ARA:ATCG00130-MON; -.
DR   PRO; PR:P56759; -.
DR   Proteomes; UP000006548; Chloroplast.
DR   ExpressionAtlas; P56759; baseline and differential.
DR   Genevisible; P56759; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0009579; C:thylakoid; HDA:TAIR.
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_0000082403"
FT   TRANSMEM        27..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
SQ   SEQUENCE   184 AA;  21057 MW;  BBC88703401D30CA CRC64;
     MKNLTDSFVY LGHWPSAGSF GFNTDILATN PINLSVVFGV LIFFGKGVLN DLLDNRKQRI
     LNTIRNSEEL REGAIQQLEN ARARLRNVET EADKFRVNGY SEIEREKLNL INSTYKTLKQ
     LENYKNETIL FEQQRTINQV RERVFQQALQ GAIGTLNSCL SNELHLRTIN ANIGMFGTMK
     EITD
 
 
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