| IED ID | IndEnz0002004825 |
| Enzyme Type ID | protease004825 |
| Protein Name |
Lon protease EC 3.4.21.53 ATP-dependent protease La |
| Gene Name | lon SDY_0293 |
| Organism | Shigella dysenteriae serotype 1 (strain Sd197) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Shigella Shigella dysenteriae Shigella dysenteriae serotype 1 (strain Sd197) |
| Enzyme Sequence | MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGVNDLFTVGTVASILQMLKLPDGTVKVLVEGLQRARISALSDNGEHFSAKAEYLESPTIDEREQEVLVRTAISQFEGYIKLNKKIPPEVLTSLNSIDDPARLADTIAAHMPLKLADKQSVLEMSDVNERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDDAPDENEALKRKIDAAKMPKEAKEKAEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVKKDLRQAQEILDTDHYGLERVKDRILEYLAVQSRVNKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNVAFSDHYLEVDYDLSDVMFVATSNSMNIPAPLLDRMEVIRLSGYTEDEKLNIAKRHLLPKQIERNALKKGELTVDDSAIIGIIRYYTREAGVRGLEREISKLCRKAVKQLLLDKSLKHIEINGDNLHDYLGVQRFDYGRADNENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINPDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPFENKRDLKENPDNAKADQDRHPVKNNEEEQTLSLQNYPSVFLFFFFFFFEAIEAFNRFTAAGLKIACPAAILSLN |
| Enzyme Length | 812 |
| Uniprot Accession Number | Q32JJ5 |
| Absorption | |
| Active Site | ACT_SITE 679; /evidence=ECO:0000255|HAMAP-Rule:MF_01973; ACT_SITE 722; /evidence=ECO:0000255|HAMAP-Rule:MF_01973 |
| Activity Regulation | ACTIVITY REGULATION: Contains an allosteric site (distinct from its active site), whose occupancy by an unfolded polypeptide leads to enzyme activation. {ECO:0000255|HAMAP-Rule:MF_01973}. |
| 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. 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, and UmuD. Its overproduction specifically inhibits translation through at least two different pathways, one of them being the YoeB-YefM toxin-antitoxin system. {ECO:0000255|HAMAP-Rule:MF_01973}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 356..363; /note=ATP; /evidence=ECO:0000255|HAMAP-Rule:MF_01973 |
| Features | Active site (2); Chain (1); Compositional bias (1); Domain (2); Nucleotide binding (1); Region (1) |
| Keywords | ATP-binding;Cytoplasm;Hydrolase;Nucleotide-binding;Protease;Reference proteome;Serine protease;Stress response |
| Interact With | |
| Induction | INDUCTION: By accumulation of abnormal proteins, such as at high temperatures. Under stress conditions. {ECO:0000255|HAMAP-Rule:MF_01973}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01973}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 90,799 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |