Detail Information for IndEnz0002017734
IED ID IndEnz0002017734
Enzyme Type ID protease017734
Protein Name ATP-dependent Clp protease ATP-binding subunit ClpX
ATP-dependent unfoldase ClpX
Gene Name clpX lopC b0438 JW0428
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MTDKRKDGSGKLLYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIREEIKEVAPHRERSALPTPHEIRNHLDDYVIGQEQAKKVLAVAVYNHYKRLRNGDTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVENIIQKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAVPPQGGRKHPQQEFLQVDTSKILFICGGAFAGLDKVISHRVETGSGIGFGATVKAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVVATLNELSEEALIQILKEPKNALTKQYQALFNLEGVDLEFRDEALDAIAKKAMARKTGARGLRSIVEAALLDTMYDLPSMEDVEKVVIDESVIDGQSKPLLIYGKPEAQQASGE
Enzyme Length 424
Uniprot Accession Number P0A6H1
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. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized and readily hydrolyzed by ClpP. Can perform chaperone functions in the absence of ClpP. {ECO:0000269|PubMed:12941278, ECO:0000269|PubMed:15371343}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 120..127; /note="ATP"; /evidence="ECO:0000255|HAMAP-Rule:MF_00175, ECO:0000269|PubMed:19914167, ECO:0000269|PubMed:23622246"
Features Beta strand (12); Chain (1); Domain (1); Helix (19); Initiator methionine (1); Metal binding (4); Mutagenesis (2); Nucleotide binding (1); Sequence conflict (1); Turn (6)
Keywords 3D-structure;ATP-binding;Chaperone;Direct protein sequencing;Host-virus interaction;Metal-binding;Nucleotide-binding;Reference proteome;Stress response;Zinc
Interact With P0A6G7; Itself; P0A9A6
Induction INDUCTION: By heat shock. Part of the clpP-clpX operon, clpX can be expressed individually from its own promoter. {ECO:0000269|PubMed:8093059}.
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D NMR spectroscopy (1); Electron microscopy (12); X-ray crystallography (12)
Cross Reference PDB 1OVX; 2DS5; 2DS6; 2DS7; 2DS8; 3HTE; 3HWS; 4I34; 4I4L; 4I5O; 4I63; 4I81; 4I9K; 6PO1; 6PO3; 6POD; 6POS; 6PP5; 6PP6; 6PP7; 6PP8; 6PPE; 6WR2; 6WRF; 6WSG;
Mapped Pubmed ID 15690043; 16606699; 19183285; 24561554; 24627523; 32108573; 33089779;
Motif
Gene Encoded By
Mass 46,356
Kinetics
Metal Binding METAL 15; /note="Zinc"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01250, ECO:0000269|PubMed:14525985"; METAL 18; /note="Zinc"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01250, ECO:0000269|PubMed:14525985"; METAL 37; /note="Zinc"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01250, ECO:0000269|PubMed:14525985"; METAL 40; /note="Zinc"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01250, ECO:0000269|PubMed:14525985"
Rhea ID
Cross Reference Brenda 3.4.21.92;