| IED ID | IndEnz0002015950 |
| Enzyme Type ID | protease015950 |
| Protein Name |
Lon protease EC 3.4.21.53 ATP-dependent protease La |
| Gene Name | lon |
| Organism | Erwinia amylovora (Fire blight bacteria) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Erwiniaceae Erwinia Erwinia amylovora (Fire blight bacteria) |
| Enzyme Sequence | MNPERSERIEIPVLPLRDVVVYPHMVIPLFVGREKSIRCLEAAMDHDKKIMLVAQKEASTDEPGINDLFSVGTVASILQMLKLPDATVKVLVEGLQRARISALSDNGDHFTAKAEYLTSPEIEEREQEVLVRTAINQFEGYIKLNKKIPPEVLTSLNSIDDAARLADTVAAHMPLKLSDKQSVLEMSDVDERLEYLMAMMESEIDLLQVEKRIRNRVKKQMEKSQREYYLNEQMKAIQKELGEMDDAPDENEALKRKIDAARMPKEAREKTEAELQKLKMMSPMSAEATVVRGYIDWMVQVPWNARSKVEKDLQKRRQTLDTDHFGLERVKDRILEYLAVQSRVSKIKGPILCLVGPPGVGKTSLGQSIAKATGRKYVRMALGGVRDEAEIRGHRRTYIGSMPGKLIQKMAKVGVKNPLFLLDEIDKMSSDMRGDPASALLEVLDPEQNIAFNDHYLEVDYDLSDVMFVATSNSMNIPAPLLDRMEVIRLSGYTEDEKLNIAKKHLLSKQIERNALKEHELIVDDSAIVGIIRYYTRERGVRSLERELSKLCRKAVKTLLMDKSVKHIEINADNLKDYLGVQRYDYGRADSENRVGQVTGLAWTEVGGDLLTIETACVPGKGKLTYTGSLGEVMQESIQAALTVVRARAEKLGINGDFYEKRDIHVHVPEGATPKDGPSAGIAMCTALVSCLTGNPVRADVAMTGEITLRGQVLPIGGLKEKLLAAHRGGIKTVLIPDENKRDLEEIPENVIADLDIHPVKRIEEVLALALQNAPYGMQVASVK |
| Enzyme Length | 784 |
| Uniprot Accession Number | P46067 |
| 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 | |
| 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. {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); Domain (2); Nucleotide binding (1) |
| Keywords | ATP-binding;Cytoplasm;Hydrolase;Nucleotide-binding;Protease;Serine protease;Stress response |
| Interact With | |
| Induction | INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973, ECO:0000269|PubMed:7860603}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 87,670 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.53; |