ClpX
| ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial | ||
|---|---|---|
| Properties of human protein | ||
| Mass / length primary structure | 633 amino acids , 69,224 Da | |
| Identifier | ||
| External IDs | ||
| Orthologue (human) | ||
| Entrez | 10845 | |
| Ensemble | ENSG00000166855 | |
| UniProt | O76031 | |
| Refseq (mRNA) | NM_006660.4 | |
| Refseq (protein) | NP_006651.2 | |
| PubMed search |
10845
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ClpX (ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial) is a protein from the group of AAA proteins .
properties
ClpX is mainly formed in the skeletal muscles and in the heart , but also in the liver , brain , placenta , lungs , kidneys and pancreas . It binds and hydrolyzes adenosine triphosphate .
ClpX strengthens the binding of DNA through TFAM . It is also necessary for the structure of the nucleoid in the mitochondrion . ClpX is a chaperone that the binding of the pyridoxal - cofactor to the 5-aminolevulinic acid synthase mediated so that the biosynthesis of 5-aminolevulinic acid (ALA) and thus as a result of heme is increased. In addition, ClpX is involved in the formation of the Clp complex from ClpA and ClpP . Six ClpX molecules also form the protease complex ClpXp with ClpP. ClpX is acetylated .
Web links
Individual evidence
- ^ TA Baker, RT Sauer: ClpXP, an ATP-powered unfolding and protein-degradation machine. In: Biochimica et Biophysica Acta . Volume 1823, number 1, January 2012, pp. 15-28, doi : 10.1016 / j.bbamcr.2011.06.007 , PMID 21736903 , PMC 3209554 (free full text).
- ^ SE Glynn, AR Nager, TA Baker, RT Sauer: Dynamic and static components power unfolding in topologically closed rings of a AAA + proteolytic machine. In: Nature structural & molecular biology. Volume 19, number 6, May 2012, pp. 616-622, doi : 10.1038 / nsmb.2288 , PMID 22562135 , PMC 3372766 (free full text).