Detail Information for IndEnz0002007527
IED ID IndEnz0002007527
Enzyme Type ID protease007527
Protein Name Lon protease
EC 3.4.21.53
ATP-dependent protease La
Gene Name lon FMG_1206
Organism Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508) (Peptostreptococcus magnus)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Firmicutes Tissierellia Tissierellales Peptoniphilaceae Finegoldia Finegoldia magna (Peptostreptococcus magnus) Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508) (Peptostreptococcus magnus)
Enzyme Sequence MKEYYTISEKKLPIIALRGLWLFPNNIQHFEVGREVSLNALNASLLRNSEIFICTQKDPMLENITKEDFYHTGVLASIKQTIKMPNGNIRVLVEAYDRAKIVDFVENDSFLEANVEVMEYDKTKYHPTDKSLTMIRMIISSFESLAEIIKKPLPQDLLGGLLNEEDPSSLIDTIAMLISLNDKDSILLLETLDMDERIELVYKFVIKEIEFLKIKEDIEERTNKEISDTQKEYFLQEQLRQIKMELGEEYDIEDTDDYANRVKKLKLKKDSEEHVLKEINRLSSMNPNNPESTVIRNYIDQVLDIPWNKKSKSSIDLKVAEKVLNDGHFGLEDVKKRILEYLAVKKMTGSLKGPILCLVGPPGVGKTSIARSIADATNRKFVSMRLGGVRDEAEIRGHRKTYIGAMPGRIITQLQKAKKLNPVFLLDEIDKLASDFRGDPASALLEVLDPEQNSEFTDNYIEIPVDLSDVLFITTANSQEQIPDALLDRMEVIRVTSYTDSEKFEIANRYLLPRQLKENGMDKSQFHITRDAIYTIINNYTRESGVRELERNIGKVIRKAVVKIVKDDVKKVVVNNKNLEKFLGSKLVLDDEIPREDTVGVVNGLAWTQVGGVILTIEANVMDGSGKTQLTGKLGDVMKESAMAAISYIRSNQEALGIKGEFYKEKDIHIHVPEGAVPKDGPSAGVTMVTALVSALTGRKVKHDFAMTGEITLTGRVLAIGGVKEKVLAAHRYGINKVFLPKENKRDIQDIDPKIRQKIKFYFTSNVKEILDEVLI
Enzyme Length 776
Uniprot Accession Number B0S2N4
Absorption
Active Site ACT_SITE 683; /evidence=ECO:0000255|HAMAP-Rule:MF_01973; ACT_SITE 726; /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 360..367; /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;Reference proteome;Serine protease;Stress response
Interact With
Induction INDUCTION: By heat shock. {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 87,866
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda