ATPF2_PHATC
ID ATPF2_PHATC Reviewed; 156 AA.
AC A0T0E8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 52.
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 Phaeodactylum tricornutum (strain CCAP 1055/1).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1;
RX PubMed=17252281; DOI=10.1007/s00438-006-0199-4;
RA Oudot-Le Secq M.-P., Grimwood J., Shapiro H., Armbrust E.V., Bowler C.,
RA Green B.R.;
RT "Chloroplast genomes of the diatoms Phaeodactylum tricornutum and
RT Thalassiosira pseudonana: comparison with other plastid genomes of the red
RT lineage.";
RL Mol. Genet. Genomics 277:427-439(2007).
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; EF067920; ABK20646.1; -; Genomic_DNA.
DR RefSeq; YP_874423.1; NC_008588.1.
DR AlphaFoldDB; A0T0E8; -.
DR SMR; A0T0E8; -.
DR STRING; 556484.A0T0E8; -.
DR PRIDE; A0T0E8; -.
DR GeneID; 4524628; -.
DR InParanoid; A0T0E8; -.
DR Proteomes; UP000000759; Chloroplast.
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 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; CF(0); Chloroplast; Hydrogen ion transport; Ion transport;
KW Membrane; Plastid; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..156
FT /note="ATP synthase subunit b', chloroplastic"
FT /id="PRO_0000369063"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01399"
SQ SEQUENCE 156 AA; 17654 MW; A9B36DB1EC9399F3 CRC64;
MINISMLISN SEVSGPGGLF DFNATLPLVA IQFILLMVLL NILLYNPLLT IIEERKEYIL
TNLGKASELL SEANKLTQQY EQELDNVRKE AQLEITNSQK IHKEILEVEL NISQKYIDNL
LDTIQKDLLA KKNIALNSLD EIVQSLCVDI EARLSI
