ID A0A7G3WHA1_ARACU Unreviewed; 184 AA.
AC A0A7G3WHA1;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 25-MAY-2022, entry version 6.
DE RecName: Full=ATP synthase subunit b, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01398};
DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000256|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I {ECO:0000256|HAMAP-Rule:MF_01398};
GN Name=atpF {ECO:0000256|HAMAP-Rule:MF_01398,
GN ECO:0000313|EMBL:QKG04187.1};
OS Araucaria cunninghamii (Hoop pine) (Moreton Bay pine).
OG Plastid; Chloroplast {ECO:0000313|EMBL:QKG04187.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Araucariales;
OC Araucariaceae; Araucaria.
OX NCBI_TaxID=56994 {ECO:0000313|EMBL:QKG04187.1};
RN [1] {ECO:0000313|EMBL:QKG04187.1}
RP NUCLEOTIDE SEQUENCE.
RA Ping J., Luo X., Zhu M., Zhang R., Qian C., Su Y., Wang T.;
RT "The complete chloroplast genome of Araucaria cunninghamii
RT (Araucariaceae).";
RL Mitochondrial DNA B Resour 5:2952-2953(2020).
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). {ECO:0000256|HAMAP-
CC Rule:MF_01398}.
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.
CC {ECO:0000256|ARBA:ARBA00025198, ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01398}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Plastid,
CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01398};
CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01398}.
CC -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as
CC CF(1)CF(0). {ECO:0000256|HAMAP-Rule:MF_01398}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000256|HAMAP-
CC Rule:MF_01398, ECO:0000256|RuleBase:RU003848}.
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DR EMBL; MT227812; QKG04187.1; -; Genomic_DNA.
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: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 {ECO:0000256|HAMAP-Rule:MF_01398};
KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01398};
KW Chloroplast {ECO:0000313|EMBL:QKG04187.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW Rule:MF_01398};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01398};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01398};
KW Plastid {ECO:0000313|EMBL:QKG04187.1};
KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01398};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01398};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01398};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01398}.
FT TRANSMEM 31..49
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01398"
FT COILED 64..98
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 104..124
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 184 AA; 20964 MW; A815ABFF720C5520 CRC64;
MKNVTDSSIS LVYWPFAGGF ELNTNIFETN IINLSVVLGV LIYFGKGVLS NLLDNRKQKI
LSTIRNSEEL CKGAANQLEQ ARARLREVEK RAGEIRLNGY SQIEREKEDF IKAASANLEQ
LEESKNETVH FEQQRAIEQV RQQVSRQAVQ RALGTLNIRL NSELHLRTID HNIGLLRAMK
NITD
//