AC MF_01416; DC Protein; auto c? or TR HAMAP; MF_01416; -; 1; level=0 XX Names: ATP_synth_delta_bact XX ID ATPD case DE RecName: Full=ATP synthase subunit delta; DE AltName: Full=ATP synthase F(1) sector subunit delta; DE AltName: Full=F-type ATPase subunit delta; DE Short=F-ATPase subunit delta; else case DE RecName: Full=ATP synthase subunit delta, chloroplastic; DE AltName: Full=ATP synthase F(1) sector subunit delta; DE AltName: Full=F-type ATPase subunit delta; end case case GN Name=atpD; else case GN Name=atpH; Synonyms=atpD; else GN Name=atpH; end case XX 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 -!- 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. case or and not and not 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. else 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 three main CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an CC alternating ring which encloses part of the gamma chain. F(1) is CC 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 and b chains. end case case CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; CC Peripheral membrane protein. else case and not CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane CC protein. else case CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. else case not defined or CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. else case CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. end case CC -!- SIMILARITY: Belongs to the ATPase delta chain family. XX DR PROSITE; PS00389; ATPASE_DELTA; 1; trigger=no DR Pfam; PF00213; OSCP; 1; trigger=no DR PRINTS; PR00125; ATPASEDELTA; 1; trigger=no DR NCBIfam; TIGR01145; ATP_synt_delta; 1; trigger=no XX KW ATP synthesis KW CF(1) KW Hydrogen ion transport KW Ion transport KW Transport case or and not KW Thylakoid else case KW Cell membrane KW Cell inner membrane else case not defined or KW Cell membrane else case KW Cell membrane KW Cell inner membrane end case KW Membrane XX GO GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism GO GO:0015986; P:proton motive force-driven ATP synthesis case GO GO:0009535; C:chloroplast thylakoid membrane else case and not GO GO:0042651; C:thylakoid membrane else GO GO:0005886; C:plasma membrane end case XX Size: 157-279; Related: None; Template: P0ABA4; P09220; P29708; P72244; P0A2Z5; Q0ZS22; Scope: Bacteria Plastid Fusion: Nter: MF_01398 (atpF) Cter: None Duplicate: in BRAHW, SYNC1, PELPD, PHOPR, VIBC1, VIBA3 Plasmid: None Comments: In some of the Mycobacteria one copy is fused with the b subunit. For a review on the peripheral (stator) stalk see PubMed=16730323; DOI=10.1016/j.bbabio.2006.04.007; Weber J.; "ATP synthase: subunit-subunit interactions in the stator stalk."; Biochim. Biophys. Acta 1757:1162-1170(2006). XX # Revision 1.19 2023/06/01 //