| 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; |