| IED ID |
IndEnz0002017573 |
| Enzyme Type ID |
protease017573 |
| Protein Name |
ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial
|
| Gene Name |
Clpx |
| Organism |
Rattus norvegicus (Rat) |
| 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
Rattus
Rattus norvegicus (Rat)
|
| Enzyme Sequence |
MSSCGACTCGAAAARLLTTSLTSAQRGISCGRIHVPVLGRLGTLDTQILRRAPLRTFSETPAYFASKDGTNKDGSGDGNKKSVTEGSSKKSGSGNSGKGGNQLRCPKCGDLCTHVETFVSSTRFVKCEKCHHFFVVLSEADSKKSIIKEPESAAEAVKLAFQQKPPPPPKKIYNYLDKYVVGQSFAKKVLSVAVYNHYKRIYNNIPANLRQQAEVEKQTSLTPRELEIRRREDEYRFTKLLQIAGISPHGNALGASMQQQGSQQMPQEKRGGEVLDSPHDDIKLEKSNILLLGPTGSGKTLLAQTLAKCLDVPFAICDCTTLTQAGYVGEDIESVIAKLLQDANYNVEKAQQGIVFLDEVDKIGSVPGIHQLRDVGGEGVQQGLLKLLEGTIVNVPEKNSRKLRGETVQVDTTNILFVASGAFNGLDRIISRRKNEKYLGFGTPSNLGKGRRAAAAADLANRSGESNTHQDIEEKDRLLRHVEARDLIEFGMIPEFVGRLPVVVPLHSLDEKTLVQILTEPRNAVIPQYQALFSMDKCELNVTEDALKAIARLALERKTGARGLRSIMEKLLLEPMFEVPNSDIVCVEVDKEVVEGKKEPGYIRAPSKESSEEDYDSGVEEDGWPRQADAANS |
| Enzyme Length |
633 |
| Uniprot Accession Number |
Q5U2U0 |
| 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. 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. {ECO:0000250|UniProtKB:O76031}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
NP_BIND 294..301; /note=ATP; /evidence=ECO:0000250 |
| Features |
Chain (1); Compositional bias (2); Domain (1); Metal binding (4); Modified residue (2); Nucleotide binding (1); Region (2); 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:0000250}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}. |
| Modified Residue |
MOD_RES 437; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:O76031; MOD_RES 617; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O76031 |
| Post Translational Modification |
|
| Signal Peptide |
|
| Structure 3D |
|
| Cross Reference PDB |
- |
| Mapped Pubmed ID |
- |
| Motif |
|
| Gene Encoded By |
|
| Mass |
69,208 |
| Kinetics |
|
| Metal Binding |
METAL 105; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 108; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 127; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 130; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250 |
| Rhea ID |
|
| Cross Reference Brenda |
|