ATPD_GUITH
ID ATPD_GUITH Reviewed; 185 AA.
AC O78476;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=ATP synthase subunit delta, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01416};
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_01416}.
CC -!- FUNCTION: This protein is part of the stalk that links CF(0) to CF(1).
CC It either transmits conformational changes from CF(0) to CF(1) or is
CC implicated in proton conduction. {ECO:0000255|HAMAP-Rule:MF_01416}.
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). CF(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_01416}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01416}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01416}.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01416}.
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DR EMBL; AF041468; AAC35667.1; -; Genomic_DNA.
DR RefSeq; NP_050733.1; NC_000926.1.
DR AlphaFoldDB; O78476; -.
DR SMR; O78476; -.
DR GeneID; 857038; -.
DR HOGENOM; CLU_085114_4_1_1; -.
DR OMA; EYDTYRM; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.520.20; -; 1.
DR HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR InterPro; IPR020781; ATPase_OSCP/d_CS.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR PANTHER; PTHR11910; PTHR11910; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF47928; SSF47928; 1.
DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
DR PROSITE; PS00389; ATPASE_DELTA; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(1); Chloroplast; Hydrogen ion transport; Ion transport;
KW Membrane; Plastid; Thylakoid; Transport.
FT CHAIN 1..185
FT /note="ATP synthase subunit delta, chloroplastic"
FT /id="PRO_0000193502"
SQ SEQUENCE 185 AA; 20219 MW; 22EF411A7E99F3F1 CRC64;
MIAMNNKLAQ PYAMAFLEFS LDAKQTLDTT IADLTQIKTI LHDSVDLSKT LSNPLLSIKA
KKEVIKAIFE PNISKNTLKF LLVLCDRGRS ANLSSIIDNT IELAYKKASI EIAYVTTATA
FSSNQQEALV EKLKSMTSTE QIKLNITVDK TLIGGFKVQI GSKVIDTSIQ GQLRQLASHL
GSSAI