HAMAP rule MF_01393
General rule information
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Accession | MF_01393 |
Dates | 28-NOV-2008 (Created)
7-DEC-2023 (Last updated, Version 25) |
Name | ATP_synth_a_bact |
Scope(s) |
Bacteria Plastid |
Template(s) | P0AB98 (ATP6_ECOLI); P06451 (ATPI_SPIOL); [ Recover all ] |
Triggered by |
case c? <OC:Bacteria> or <OG:Chloroplast>
HAMAP; MF_01393 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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case <OC:Bacteria> | |
Identifier | ATP6 |
Protein name | RecName: Full=ATP synthase subunit a; AltName: Full=ATP synthase F0 sector subunit a; AltName: Full=F-ATPase subunit 6; |
else case <OG:Chloroplast> | |
Identifier | ATPI |
Protein name | RecName: Full=ATP synthase subunit a, chloroplastic; AltName: Full=ATP synthase F0 sector subunit a; AltName: Full=F-ATPase subunit IV; |
end case | |
case <OC:Cyanobacteriota> | |
Gene name | Name=atpB; Synonyms=atpI; |
else case <OG:Chloroplast> | |
Gene name | Name=atpI; |
else | |
Gene name | Name=atpB; |
end case |
Comments
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FUNCTION | Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. |
case <OG:Chloroplast> or <Property:PHOTOSYN> | |
SUBUNIT | F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a, b, b' and c. |
else | |
SUBUNIT | F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(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 | |
SIMILARITY | Belongs to the ATPase A chain family. |
Keywords
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ATP synthesis | |
CF(0) | |
Hydrogen ion transport | |
Ion transport | |
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 | |
GO:0015986; Biological process:proton motive force-driven ATP synthesis | |
case <OCellular component:Cyanobacteriota> and not <OC:Gloeobacter> | |
GO:0042651; Cellular component:thylakoid membrane | |
else; https://www.ebi.ac.uk/QuickGO/term/else | |
GO:0005886; Cellular component:plasma membrane | |
end case | |
case <OG:Chloroplast> | |
GO:0009535; Cellular component:chloroplast thylakoid membrane | |
end case |
Cross-references
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PROSITE | PS00449; ATPASE_A; 1; |
Pfam | PF00119; ATP-synt_A; 1; |
PRINTS | PR00123; ATPASEA; 1; |
NCBIfam | TIGR01131; ATP_synt_6_or_A; 1; |
General | Transmembrane; -; 4-8; |
Features
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Additional information
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Size range | 207-406 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |
Comments | In Anaeromyxobacter and some of the Chlorobiota the protein could have a signal sequence; these proteins have a considerably longer N- terminus compared to other family members. |