IED ID | IndEnz0002004943 |
Enzyme Type ID | protease004943 |
Protein Name |
Lon protease EC 3.4.21.53 ATP-dependent protease La |
Gene Name | lon Csac_1506 |
Organism | Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T 6331) |
Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Firmicutes Clostridia Thermoanaerobacterales Thermoanaerobacterales Family III. Incertae Sedis Caldicellulosiruptor Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum) Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T 6331) |
Enzyme Sequence | MMIAVTKRTIPVIPLRGLVVFPYMMLHFDVGRQISLKALEEAMNSDQQVLLLAQKDPKQEEPSPEDLYQYGTVAKIKQMLKLPSETSRILVEGLSRAKVIGYVSVDPYFLVEVEEYKEKGGNLDDPELEALIRNVVSAFEEYARLTSRIPPDAILSVTTIQNPGQLADVIAANVIVKLEDKQLLLEQVDLKERLTKLYELILREKEIIEIERKITIKVKKQIDKMQKEYYLREQLKAIQSELGEKDSLFSEAQEYREQVQKLGLSNENLQKVYKEIDRLEKLPPNSPEIGVIRTYLEWIIDLPWNVKSEEKIDINVVKNVLDEDHYGLTKVKERILEYIAVRKLKNNLKGPILCLVGPPGVGKTSIAKSIARALNRNYVRISLGGLRDEAEIRGHRKTYVGAMPGRIIYALRQAKTKNPLILLDEIDKMSQDFRGDPASALLEVLDSEQNYAFRDHYVEIPFDLSEVMFIATANTLETIPRPLLDRLEVIEITGYTEEEKVEIAKRYLFPKQIEQNGLKKSQIRYDEAVIRDIISFYTRESGVRNLEREIARLCRRVAKEILEENKKMVRITTRNLEKYLGVRKYRRDELIEEDRIGIVTGLAWTPFGGETLSVEALVMPGSGKLELTGQLGDVMKESAKAAVSIIRARAKELGIDENFYKEYDIHIHVPEGAIPKDGPSAGVTMATAMVSALSKKPVRHDVAMTGEITLSGRVLPIGGVKEKILAAKRVGIKNVILPYENKKDVDELEDYVKKDMNFVFVKAIDEVFKIAIKE |
Enzyme Length | 774 |
Uniprot Accession Number | A4XJL4 |
Absorption | |
Active Site | ACT_SITE 680; /evidence=ECO:0000255|HAMAP-Rule:MF_01973; ACT_SITE 723; /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 357..364; /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}. |
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 | 88,114 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |