| IED ID | IndEnz0002006509 |
| Enzyme Type ID | protease006509 |
| Protein Name |
Desampylase EC 3.4.19.15 HvJAMM1 |
| Gene Name | HVO_2505 C498_07813 |
| Organism | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Stenosarchaea group Halobacteria Haloferacales Haloferacaceae Haloferax Haloferax volcanii (Halobacterium volcanii) Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) |
| Enzyme Sequence | MTSSRLSLAADARDSILSHAREGAAGDPPAEVCGVLAGDSDARTVTAAHPVSNVAAEPRVAYELDPEETVSILEAIESAGDDAVGFYHSHPESDPVPSATDRERASWPGYVYLICSPDGRMTAHEWTGDEFRELSVAVE |
| Enzyme Length | 139 |
| Uniprot Accession Number | D4GTS4 |
| Absorption | |
| Active Site | ACT_SITE 31; /note=Proton donor/acceptor; /evidence=ECO:0000305|PubMed:22970855 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and N-ethylmaleimide (NEM) in vitro. {ECO:0000269|PubMed:22970855}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=An N(6)-[small archaeal modifier protein]-[protein]-L-lysine + H(2)O = a [protein]-L-lysine + a [small archaeal modifier protein].; EC=3.4.19.15; Evidence={ECO:0000269|PubMed:22970855}; |
| DNA Binding | |
| EC Number | 3.4.19.15 |
| Enzyme Function | FUNCTION: Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. Functions as a specific and not a general protease since it is unable to hydrolyze a variety of unmodified proteins otherwise hydrolyzed by proteinase K. {ECO:0000269|PubMed:22970855, ECO:0000269|PubMed:24097257}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-50 degrees Celsius. Is active over a wide range of temperature (20-60 degrees Celsius). However, the enzyme is not active at 70 degrees Celsius. {ECO:0000269|PubMed:22970855}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-10. Displays little to no activity at low pH (pH 6.5 and below). {ECO:0000269|PubMed:22970855}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (1); Metal binding (3); Motif (1); Mutagenesis (7); Site (1) |
| Keywords | Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 88..101; /note=JAMM motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Gene Encoded By | |
| Mass | 14,739 |
| Kinetics | |
| Metal Binding | METAL 88; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 90; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182; METAL 101; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01182 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.19.15; |