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ATP synthase subunit b, chloroplastic (ATP synthase F(0) sector subunit b) (ATPase subunit I)

 H2F4S5_9ASPA            Unreviewed;       184 AA.
H2F4S5;
21-MAR-2012, integrated into UniProtKB/TrEMBL.
21-MAR-2012, sequence version 1.
27-SEP-2017, entry version 27.
RecName: Full=ATP synthase subunit b, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01398};
AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
AltName: Full=ATPase subunit I {ECO:0000256|HAMAP-Rule:MF_01398};
Name=atpF {ECO:0000256|HAMAP-Rule:MF_01398,
ECO:0000313|EMBL:AEX93658.1};
Hosta ventricosa (blue plantain lily).
Plastid; Chloroplast {ECO:0000313|EMBL:AEX93658.1}.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Asparagaceae;
Agavoideae; Hosta.
NCBI_TaxID=39527 {ECO:0000313|EMBL:AEX93658.1};
[1] {ECO:0000313|EMBL:AEX93658.1}
NUCLEOTIDE SEQUENCE.
PubMed=22291168; DOI=10.3732/ajb.1100491;
Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J.,
Pires J.C.;
"Quality and quantity of data recovered from massively parallel
sequencing: Examples in Asparagales and Poaceae.";
Am. J. Bot. 99:330-348(2012).
[2] {ECO:0000313|EMBL:APO12208.1}
NUCLEOTIDE SEQUENCE.
PubMed=27793858;
McKain M.R., McNeal J.R., Kellar P.R., Eguiarte L.E., Pires J.C.,
Leebens-Mack J.;
"Timing of rapid diversification and convergent origins of active
pollination within Agavoideae (Asparagaceae).";
Am. J. Bot. 103:1717-1729(2016).
-!- FUNCTION: Component of the F(0) channel, it forms part of the
peripheral stalk, linking F(1) to F(0). {ECO:0000256|HAMAP-
Rule:MF_01398}.
-!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the
presence of a proton or sodium gradient. F-type ATPases consist of
two structural domains, F(1) containing the extramembraneous
catalytic core and F(0) containing the membrane proton channel,
linked together by a central stalk and a peripheral stalk. During
catalysis, ATP synthesis in the catalytic domain of F(1) is
coupled via a rotary mechanism of the central stalk subunits to
proton translocation. {ECO:0000256|HAMAP-Rule:MF_01398}.
-!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic
core - and F(0) - the membrane proton channel. F(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0)
has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha
and beta chains form an alternating ring which encloses part of
the gamma chain. F(1) is attached to F(0) by a central stalk
formed by the gamma and epsilon chains, while a peripheral stalk
is formed by the delta, b and b' chains. {ECO:0000256|HAMAP-
Rule:MF_01398}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000256|HAMAP-Rule:MF_01398}; Single-pass membrane protein
{ECO:0000256|HAMAP-Rule:MF_01398}.
-!- MISCELLANEOUS: In plastids the F-type ATPase is also known as
CF(1)CF(0). {ECO:0000256|HAMAP-Rule:MF_01398}.
-!- SIMILARITY: Belongs to the ATPase B chain family.
{ECO:0000256|HAMAP-Rule:MF_01398, ECO:0000256|RuleBase:RU003848}.
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EMBL; JQ273695; AEX93658.1; -; Genomic_DNA.
EMBL; KX931460; APO12208.1; -; Genomic_DNA.
RefSeq; YP_009335150.1; NC_032706.1.
GeneID; 30766897; -.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule.
HAMAP; MF_01398; ATP_synth_b_bprime; 1.
InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
Pfam; PF00430; ATP-synt_B; 1.
3: Inferred from homology;
ATP synthesis {ECO:0000256|HAMAP-Rule:MF_01398};
CF(0) {ECO:0000256|HAMAP-Rule:MF_01398,
ECO:0000256|RuleBase:RU003848};
Chloroplast {ECO:0000313|EMBL:AEX93658.1};
Coiled coil {ECO:0000256|SAM:Coils};
Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01398,
ECO:0000256|RuleBase:RU003848};
Ion transport {ECO:0000256|HAMAP-Rule:MF_01398,
ECO:0000256|RuleBase:RU003848};
Membrane {ECO:0000256|HAMAP-Rule:MF_01398};
Plastid {ECO:0000313|EMBL:AEX93658.1};
Thylakoid {ECO:0000256|HAMAP-Rule:MF_01398};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_01398};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01398};
Transport {ECO:0000256|HAMAP-Rule:MF_01398,
ECO:0000256|RuleBase:RU003848}.
TRANSMEM 32 49 Helical. {ECO:0000256|HAMAP-
Rule:MF_01398}.
COILED 64 98 {ECO:0000256|SAM:Coils}.
SEQUENCE 184 AA; 20861 MW; 5AAE9BAAD8B8AD85 CRC64;
MQNVTDSFVS LGRWPSAGSF GFNTDILATN PINLSVVLGV LIYFGKGVLN DLLDNRKQRI
LSTIRNSEEL RRGAIEQLER ARARLRKVEM EADEYRMNGY SEIEREKANL INATSDSLEQ
LENYKNETLH FEQQRAINQV RQQVFQQALQ GALGTLNSCL NSELHFRTIN ANIGILGAME
EITD


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