Summary: ATP12 chaperone protein
ATP12 chaperone protein Provide feedback
Mitochondrial F1-ATPase is an oligomeric enzyme composed of five distinct subunit polypeptides. The alpha and beta subunits make up the bulk of protein mass of F1. In Saccharomyces cerevisiae both subunits are synthesised as precursors with amino-terminal targeting signals that are removed upon translocation of the proteins to the matrix compartment . These proteins include examples from eukaryotes and bacteria and may have chaperone activity, being involved in F1 ATPase complex assembly.
Wang ZG, Sheluho D, Gatti DL, Ackerman SH; , EMBO J 2000;19:1486-1493.: The alpha-subunit of the mitochondrial F(1) ATPase interacts directly with the assembly factor Atp12p. PUBMED:10747017 EPMC:10747017
Bowman S, Ackerman SH, Griffiths DE, Tzagoloff A; , J Biol Chem 1991;266:7517-7523.: Characterization of ATP12, a yeast nuclear gene required for the assembly of the mitochondrial F1-ATPase. PUBMED:1826907 EPMC:1826907
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR011419
This entry represents a group of ATPase F1F0-assembly proteins, including ATP12 and ATPAF2 (ATP synthase mitochondrial F1 complex assembly factor 2). These proteins are essential for the assembly of the mitochondrial F1-F0 complex.
Mitochondrial F1-ATPase is an oligomeric enzyme composed of five distinct subunit polypeptides. The alpha and beta subunits make up the bulk of protein mass of F1. In Saccharomyces cerevisiae both subunits are synthesised as precursors with N-terminal targeting signals that are removed upon translocation of the proteins to the matrix compartment [PUBMED:1826907]. These proteins include examples from eukaryotes and bacteria and may have chaperone activity, being involved in F1 ATPase complex assembly.
|Biological process||proton-transporting ATP synthase complex assembly (GO:0043461)|
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Curation and family details
|Seed source:||Pfam-B_6737 (release 11.0)|
|Author:||Wood V, Studholme DJ|
|Number in seed:||260|
|Number in full:||1333|
|Average length of the domain:||125.10 aa|
|Average identity of full alignment:||37 %|
|Average coverage of the sequence by the domain:||43.39 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the ATP12 domain has been found. There are 7 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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