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HAMAP rule MF_01396

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_01396
Accession MF_01396
Dates 30-JAN-2009 (Created)
01-JUN-2023 (Last updated, Version 23)
Name ATP_synth_c_bact
Scope(s) Bacteria
Plastid
Template(s) P68699; Q8KRV3; P00845; P69447; [ Recover all ]
Triggered by HAMAP; MF_01396 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

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 [?]

FUNCTIONF(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.
FUNCTIONKey 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>
SUBUNITF-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
SUBUNITF-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 LOCATIONPlastid, chloroplast thylakoid membrane; Multi- pass membrane protein.
else case <OC:Cyanobacteriota> and not <OC:Gloeobacter>
SUBCELLULAR LOCATIONCellular thylakoid membrane; Multi-pass membrane protein.
else case <OC:Gloeobacter>
SUBCELLULAR LOCATIONCell inner membrane; Multi-pass membrane protein.
else case not defined <Property:Membrane> or <Property:Membrane=1>
SUBCELLULAR LOCATIONCell membrane; Multi-pass membrane protein.
else case <Property:Membrane=2>
SUBCELLULAR LOCATIONCell inner membrane; Multi-pass membrane protein.
end case
case <OG:Chloroplast>
MISCELLANEOUSIn plastids the F-type ATPase is also known as CF(1)CF(0).
end case
SIMILARITYBelongs to the ATPase C chain family.

Keywords [?]

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 [?]

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 [?]

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 [?]

From: ATPL_ECOLI (P68699)
Key From To Description Tag Condition FTGroup
SITE 61 61 /note="Reversibly protonated during proton transport" [DE]

Additional information [?]

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.



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