ATPF2_GUITH
ID ATPF2_GUITH Reviewed; 163 AA.
AC O78478;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=ATP synthase subunit b', chloroplastic {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};
OS Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG Plastid; Chloroplast.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=55529;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Leitsch C.E.W., Kowallik K.V., Douglas S.E.;
RT "The atpA gene cluster of a cryptomonad, Guillardia theta: a piece in the
RT puzzle of chloroplast genome development.";
RL J. Phycol. 35:128-135(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9929392; DOI=10.1007/pl00006462;
RA Douglas S.E., Penny S.L.;
RT "The plastid genome of the cryptophyte alga, Guillardia theta: complete
RT sequence and conserved synteny groups confirm its common ancestry with red
RT algae.";
RL J. Mol. Evol. 48:236-244(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_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, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01399}; 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}.
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DR EMBL; AF041468; AAC35669.1; -; Genomic_DNA.
DR RefSeq; NP_050735.1; NC_000926.1.
DR AlphaFoldDB; O78478; -.
DR SMR; O78478; -.
DR GeneID; 857040; -.
DR HOGENOM; CLU_079215_9_0_1; -.
DR OMA; RVAMANM; -.
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 HAMAP; MF_01399; ATP_synth_bprime; 1.
DR InterPro; IPR034679; ATP_synth_b.
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; Thylakoid;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..163
FT /note="ATP synthase subunit b', chloroplastic"
FT /id="PRO_0000082435"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01399"
SQ SEQUENCE 163 AA; 18329 MW; D3D84A154FD5A94C CRC64;
MTNYLYILAL QIAEAESEGG LFDFNATLPL MAVQILLFMV ILNAVFYNPV AKVLDEREEY
IRKNLTQASD ILAKAEAITK QYEKDLAQER REAQLIISVA QKEAQDIVAL EIKQAQKDTE
LLVNEATSQL NSQKQKALSA LEDQVNTLTE QIKSKLLSNQ LIS
