AC MF_01396; DC Protein; auto TR HAMAP; MF_01396; -; 1; level=0 XX Names: ATP_synth_c_bact XX case ID ATPL DE RecName: Full=ATP synthase subunit c; DE AltName: Full=ATP synthase F(0) sector subunit c; DE AltName: Full=F-type ATPase subunit c; DE Short=F-ATPase subunit c; DE AltName: Full=Lipid-binding protein; else case ID ATPH DE RecName: Full=ATP synthase subunit c, chloroplastic; DE AltName: Full=ATP synthase F(0) sector subunit c; DE AltName: Full=ATPase subunit III; DE AltName: Full=F-type ATPase subunit c; DE Short=F-ATPase subunit c; DE AltName: Full=Lipid-binding protein; end case case GN Name=atpH; else case GN Name=atpE; Synonyms=atpH; else GN Name=atpE; 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: Key component of the F(0) channel; it plays a direct role in CC translocation across the membrane. A homomeric c-ring of between 10-14 CC subunits forms the central stalk rotor element with the F(1) delta and CC epsilon subunits. case or 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. 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; Multi- CC pass membrane protein. else case and not CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane CC protein. else case CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. else case not defined or CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. else case CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. end case case CC -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as CC CF(1)CF(0). end case CC -!- SIMILARITY: Belongs to the ATPase C chain family. XX DR PROSITE; PS00605; ATPASE_C; 1; trigger=no DR Pfam; PF00137; ATP-synt_C; 1; trigger=no DR PRINTS; PR00124; ATPASEC; 1; trigger=no DR PRINTS; PR00122; VACATPASE; 1; trigger=no DR NCBIfam; TIGR01260; ATP_synt_c; 1; trigger=no DR General; Transmembrane; -; 2; trigger=yes XX KW ATP synthesis KW CF(0) KW Hydrogen ion transport KW Ion transport KW Lipid-binding KW Membrane KW Transmembrane 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 Transmembrane helix XX GO GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism case and not GO GO:0042651; C:thylakoid membrane else case GO GO:0009535; C:chloroplast thylakoid membrane else GO GO:0015986; P:proton motive force-driven ATP synthesis GO GO:0005886; C:plasma membrane end case XX FT From: ATPL_ECOLI (P68699) FT SITE 61 FT /note="Reversibly protonated during proton transport" FT Condition: [DE] XX Size: 66-115; Related: None; Template: P68699; Q8KRV3; P00845; P69447; Scope: Bacteria Plastid Fusion: Nter: None Cter: None Duplicate: in SYNC1, PELPD, CERS1 Plasmid: None Comments: For a review see : PubMed=18515057; DOI=10.1016/j.abb.2008.05.004; Nakamoto R.K., Baylis Scanlon J.A., Al-Shawi M.K.; "The rotary mechanism of the ATP synthase."; Arch. Biochem. Biophys. 476:43-50(2008). The number of subunits in this proton turbine determines the H+/ATP ratio and therefore the efficiency of energy conversion (PubMed:18206981). The K subunit of the V-type sodium ATPase of Enterococcus hirae, and probably other organisms, may fall into this family. However they have 2 ATP c synthase domains, whereas the non V-type subunits only have 1. Thus they have not been currently included in this family. STROR has a low score against the profile and has been made atypical. XX # Revision 1.22 2023/06/01 //