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MT000809

UniProt Annotations

Entry Information

Gene Name	caseinolytic mitochondrial matrix peptidase chaperone subunit
Protein Entry	CLPX_HUMAN
UniProt ID	O76031
Species	Human

Comments

Comment type	Description
Function	ATP-dependent specificity component of the Clp protease complex. Hydrolyzes ATP. Targets specific substrates for degradation by the Clp complex. Can perform chaperone functions in the absence of CLPP. Enhances the DNA-binding activity of TFAM and is required for maintaining a normal mitochondrial nucleoid structure. {ECO:0000269\|PubMed:11923310, ECO:0000269\|PubMed:22710082, ECO:0000269\|PubMed:22841477}.
Similarity	Belongs to the ClpX chaperone family. {ECO:0000305}.
Subcellular Location	Mitochondrion. Mitochondrion matrix, mitochondrion nucleoid.
Subunit	Homohexamer that forms a ring structure; this hexamerization requires ATP binding. Component of the Clp complex formed by the assembly of two CLPP heptameric rings with two CLPX hexameric rings, giving rise to a symmetrical structure with two central CLPP rings flanked by a CLPX ring at either end of the complex. Interacts with TFAM. {ECO:0000269\|PubMed:11923310, ECO:0000269\|PubMed:15522782, ECO:0000269\|PubMed:16115876, ECO:0000269\|PubMed:22710082, ECO:0000269\|PubMed:22841477}.
Tissue Specificity	Higher expression in skeletal muscle and heart and to a lesser extent in liver, brain, placenta, lung, kidney and pancreas. {ECO:0000269\|PubMed:11003706}.