HAMAP rule MF_01396
General rule information
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Accession | MF_01396 |
Dates | 30-JAN-2009 (Created)
1-JUN-2023 (Last updated, Version 22) |
Name | ATP_synth_c_bact |
Scope(s) |
Bacteria Plastid |
Template(s) | P68699 (ATPL_ECOLI); Q8KRV3 (ATPL_ILYTA); P00845 (ATPL_BACP3); P69447 (ATPH_SPIOL); [ Recover all ] |
Triggered by |
HAMAP; MF_01396 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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case <OC:Bacteria> | |
Identifier | ATPL |
Protein name | RecName: Full=ATP synthase subunit c; AltName: Full=ATP synthase F(0) sector subunit c; AltName: Full=F-type ATPase subunit c; Short=F-ATPase subunit c; AltName: Full=Lipid-binding protein; |
else case <OG:Chloroplast> | |
Identifier | ATPH |
Protein name | RecName: Full=ATP synthase subunit c, chloroplastic; AltName: Full=ATP synthase F(0) sector subunit c; AltName: Full=ATPase subunit III; AltName: Full=F-type ATPase subunit c; Short=F-ATPase subunit c; AltName: Full=Lipid-binding protein; |
end case | |
case <OG:Chloroplast> | |
Gene name | Name=atpH; |
else case <OC:Cyanobacteriota> | |
Gene name | Name=atpE; Synonyms=atpH; |
else | |
Gene name | Name=atpE; |
end case |
Comments
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FUNCTION | F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. |
FUNCTION | Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. |
case <OG:Chloroplast> or <Property:PHOTOSYN> | |
SUBUNIT | F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains. |
else | |
SUBUNIT | F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. |
end case | |
case <OG:Chloroplast> | |
SUBCELLULAR LOCATION | Plastid, chloroplast thylakoid membrane; Multi- pass membrane protein. |
else case <OC:Cyanobacteriota> and not <OC:Gloeobacter> | |
SUBCELLULAR LOCATION | Cellular thylakoid membrane; Multi-pass membrane protein. |
else case <OC:Gloeobacter> | |
SUBCELLULAR LOCATION | Cell inner membrane; Multi-pass membrane protein. |
else case not defined <Property:Membrane> or <Property:Membrane=1> | |
SUBCELLULAR LOCATION | Cell membrane; Multi-pass membrane protein. |
else case <Property:Membrane=2> | |
SUBCELLULAR LOCATION | Cell inner membrane; Multi-pass membrane protein. |
end case | |
case <OG:Chloroplast> | |
MISCELLANEOUS | In plastids the F-type ATPase is also known as CF(1)CF(0). |
end case | |
SIMILARITY | Belongs to the ATPase C chain family. |
Keywords
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ATP synthesis | |
CF(0) | |
Hydrogen ion transport | |
Ion transport | |
Lipid-binding | |
Membrane | |
Transmembrane | |
Transport | |
case <OG:Chloroplast> or <OC:Cyanobacteriota> and not <OC:Gloeobacter> | |
Thylakoid | |
else case <OC:Gloeobacter> | |
Cell membrane | |
Cell inner membrane | |
else case not defined <Property:Membrane> or <Property:Membrane=1> | |
Cell membrane | |
else case <Property:Membrane=2> | |
Cell membrane | |
Cell inner membrane | |
end case | |
Transmembrane helix |
Gene Ontology
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GO:0046933; Molecular function:proton-transporting ATP synthase activity, rotational mechanism | |
case <OCellular component:Cyanobacteriota> and not <OC:Gloeobacter> | |
GO:0042651; Cellular component:thylakoid membrane | |
else case <OG:Chloroplast> | |
GO:0009535; Cellular component:chloroplast thylakoid membrane | |
else; https://www.ebi.ac.uk/QuickGO/term/else | |
GO:0015986; Biological process:proton motive force-driven ATP synthesis | |
GO:0005886; Cellular component:plasma membrane | |
end case |
Cross-references
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PROSITE | PS00605; ATPASE_C; 1; |
Pfam | PF00137; ATP-synt_C; 1; |
PRINTS | PR00124; ATPASEC; 1; |
PRINTS | PR00122; VACATPASE; 1; |
NCBIfam | TIGR01260; ATP_synt_c; 1; |
General | Transmembrane; -; 2; |
Features
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From: ATPL_ECOLI (P68699) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
SITE | 61 | 61 | /note="Reversibly protonated during proton transport" | [DE] |
Additional information
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Size range | 66-115 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: 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. |