Detail Information for IndEnz0002017592
IED ID IndEnz0002017592
Enzyme Type ID protease017592
Protein Name ATP-dependent Clp protease ATP-binding subunit ClpX
Gene Name clpX CBUD_0753
Organism Coxiella burnetii (strain Dugway 5J108-111)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Legionellales Coxiellaceae Coxiella Coxiella burnetii Coxiella burnetii (strain Dugway 5J108-111)
Enzyme Sequence MSSDEKLQILYCSFCGKSQHQVRKLIAGPAVFVCNECVDLCNDIIREEEIAQAGGAQKKLPTPPEIHRMLDEYVIGQEFAKKVLSVAVYNHYKRLGNQTKKDSVEISKSNILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTEAGYVGEDVENIIQKLLQKCNYDVEKAKTGIIYIDEIDKIARKTDSPSLTRDVSGEGVQQALLKLIEGTVASIPPQGGRKHPQQEYLQVDTSNILFICGGAFADLHKIIQRRTDKIGIGFAAEVRPKEDFSREASKLIKQTEPGDLIKYGLIPEFVGRLPIITTLEELDEDALMRILTEPKNALVKQYRKLFEFEGVEIDFREDALKAIAKRAIQQKTGARGLRSIVEHTLLDLMYDLPGVAAGLRKVVIDSGVIDQASPPIFIYHHEKASRKVAQE
Enzyme Length 422
Uniprot Accession Number A9KDS7
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. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. {ECO:0000255|HAMAP-Rule:MF_00175}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 116..123; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_00175
Features Chain (1); Domain (1); Metal binding (4); Nucleotide binding (1)
Keywords ATP-binding;Chaperone;Metal-binding;Nucleotide-binding;Zinc
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 46,794
Kinetics
Metal Binding METAL 12; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 15; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 34; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 37; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250
Rhea ID
Cross Reference Brenda