| IED ID | IndEnz0002006079 |
| Enzyme Type ID | protease006079 |
| Protein Name |
Lon protease EC 3.4.21.53 ATP-dependent protease La |
| Gene Name | lon capR deg lopA muc b0439 JW0429 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRGLEREISKLCRKAVKQLLLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLEEIPDNVIADLDIHPVKRIEEVLTLALQNEPSGMQVVTAK |
| Enzyme Length | 784 |
| Uniprot Accession Number | P0A9M0 |
| Absorption | |
| Active Site | ACT_SITE 679; ACT_SITE 722; /evidence="ECO:0000255|HAMAP-Rule:MF_01973, ECO:0000269|PubMed:14665623" |
| Activity Regulation | ACTIVITY REGULATION: Contains an allosteric site (distinct from its active site), whose occupancy by an unfolded polypeptide leads to enzyme activation. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; Evidence={ECO:0000255|HAMAP-Rule:MF_01973}; |
| DNA Binding | |
| EC Number | 3.4.21.53 |
| Enzyme Function | FUNCTION: ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins, including some antitoxins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator SoxS, UmuD and at least type II antitoxins CcdA, HipB and MazE (PubMed:8022284, PubMed:16460757, PubMed:22720069, PubMed:24375411). Its overproduction specifically inhibits translation through at least two different pathways, one of them being the YoeB-YefM toxin-antitoxin system (PubMed:15009896). {ECO:0000269|PubMed:12135363, ECO:0000269|PubMed:15009896, ECO:0000269|PubMed:16460757, ECO:0000269|PubMed:16584195, ECO:0000269|PubMed:19721064, ECO:0000269|PubMed:22720069, ECO:0000269|PubMed:24375411, ECO:0000269|PubMed:8022284}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 356..363; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_01973 |
| Features | Active site (2); Beta strand (31); Chain (1); Domain (2); Erroneous initiation (1); Frameshift (1); Helix (28); Initiator methionine (1); Mutagenesis (6); Nucleotide binding (1); Sequence conflict (6); Turn (10) |
| Keywords | 3D-structure;ATP-binding;Cytoplasm;Direct protein sequencing;Hydrolase;Nucleotide-binding;Protease;Reference proteome;Serine protease;Stress response |
| Interact With | P0A7R1; P33225 |
| Induction | INDUCTION: By accumulation of abnormal proteins, such as at high temperatures. Under stress conditions. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (1); X-ray crystallography (6) |
| Cross Reference PDB | 1QZM; 1RR9; 1RRE; 2ANE; 3LJC; 6N2I; 6U5Z; |
| Mapped Pubmed ID | 11856303; 15690043; 16606699; 20693685; 24211448; 24561554; 31237118; 8910366; |
| Motif | |
| Gene Encoded By | |
| Mass | 87,438 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.201 mM for ATP for ATPase activity {ECO:0000269|PubMed:15560777}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.53;3.6.4.7; |