Detail Information for IndEnz0002018096
IED ID IndEnz0002018096
Enzyme Type ID protease018096
Protein Name ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial
Gene Name Clpx
Organism Mus musculus (Mouse)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MSSCGACTCGAAAARLLTTSLTSAQRGISCGRIHVPVLGRLGTTLDAQALRRAPLRTFSETPAYFASKDGANKDGSGDGNKKSVTEGSSKKSGSGNSGKGGNQLRCPKCGDLCTHVETFVSSTRFVKCEKCHHFFVVLSEADSKKSIIKEPESAAEAVKLAFQQKPPPPPKKIYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNIPANLRQQAEAEKQTSLTPRELEIRRREDEYRFTKLLQIAGISPHGNALGASMQQQVNQQMPQEKRGGEVLDSSQDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANYNVEKAQQGIVFLDEVDKIGSVPGIHQLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRKLRGETVQVDTTNVLFVASGAFNGLDRIISRRKNEKYLGFGTPSNLGKGRRAAAAADLANRSGESNTHQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPNSDIVCVEVDKEVVEGKKEPGYIRAPSKESSEEEYDSGVEEDGWPRQADAANS
Enzyme Length 634
Uniprot Accession Number Q9JHS4
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function 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 (PubMed:10347188). ATP-dependent unfoldase that stimulates the incorporation of the pyridoxal phosphate cofactor into 5-aminolevulinate synthase, thereby activating 5-aminolevulinate (ALA) synthesis, the first step in heme biosynthesis. Important for efficient erythropoiesis through up-regulation of heme biosynthesis (By similarity). {ECO:0000250|UniProtKB:O76031, ECO:0000269|PubMed:10347188}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 295..302; /note=ATP
Features Chain (1); Compositional bias (2); Domain (1); Metal binding (4); Modified residue (2); Mutagenesis (1); Nucleotide binding (1); Region (2); Sequence conflict (5); Transit peptide (1)
Keywords ATP-binding;Acetylation;Chaperone;Metal-binding;Mitochondrion;Mitochondrion nucleoid;Nucleotide-binding;Phosphoprotein;Reference proteome;Transit peptide;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22710082}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}.
Modified Residue MOD_RES 438; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O76031; MOD_RES 618; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O76031
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10725249; 12466851; 12865426; 12904583; 14610273; 14651853; 16141072; 18614015; 21267068; 23851121; 24194600; 26142927; 32376682; 32467259; 34280433; 34943861;
Motif
Gene Encoded By
Mass 69,229
Kinetics
Metal Binding METAL 106; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 109; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 128; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 131; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250
Rhea ID
Cross Reference Brenda