Detail Information for IndEnz0002018143
IED ID IndEnz0002018143
Enzyme Type ID protease018143
Protein Name ATP-dependent Clp protease ATP-binding subunit ClpX
Gene Name clpX Rv2457c MTV008.13c
Organism Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex Mycobacterium tuberculosis Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Enzyme Sequence MARIGDGGDLLKCSFCGKSQKQVKKLIAGPGVYICDECIDLCNEIIEEELADADDVKLDELPKPAEIREFLEGYVIGQDTAKRTLAVAVYNHYKRIQAGEKGRDSRCEPVELTKSNILMLGPTGCGKTYLAQTLAKMLNVPFAIADATALTEAGYVGEDVENILLKLIQAADYDVKRAETGIIYIDEVDKIARKSENPSITRDVSGEGVQQALLKILEGTQASVPPQGGRKHPHQEFIQIDTTNVLFIVAGAFAGLEKIIYERVGKRGLGFGAEVRSKAEIDTTDHFADVMPEDLIKFGLIPEFIGRLPVVASVTNLDKESLVKILSEPKNALVKQYIRLFEMDGVELEFTDDALEAIADQAIHRGTGARGLRAIMEEVLLPVMYDIPSRDDVAKVVVTKETVQDNVLPTIVPRKPSRSERRDKSA
Enzyme Length 426
Uniprot Accession Number P9WPB9
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 (By similarity). Degrades anti-sigma-D factor RsdA when present in a complex with ClpP1 and ClpP2. Does not seem to act on anti-sigma-L factor RslA. {ECO:0000255|HAMAP-Rule:MF_00175, ECO:0000269|PubMed:23314154}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 122..129; /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;Reference proteome;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 46,783
Kinetics
Metal Binding METAL 13; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 16; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 35; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250; METAL 38; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU01250
Rhea ID
Cross Reference Brenda