D4GTS4 · JAMM1_HALVD
- ProteinDesampylase
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids139 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Miscellaneous
Is optimally active at NaCl concentrations of 0.7-2 M, and displays little to no activity at low concentrations of salt (150 mM NaCl).
Catalytic activity
Cofactor
Note: Binds 1 zinc ion per subunit.
Activity regulation
Inhibited by EDTA and N-ethylmaleimide (NEM) in vitro.
pH Dependence
Optimum pH is 7-10. Displays little to no activity at low pH (pH 6.5 and below).
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.
Features
Showing features for active site, binding site, site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metalloexopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDesampylase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Haloferacaceae > Haloferax
Accessions
- Primary accessionD4GTS4
Proteomes
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 31 | Loss of catalytic activity. | ||||
Sequence: E → D | ||||||
Mutagenesis | 88 | Loss of catalytic activity. | ||||
Sequence: H → N | ||||||
Mutagenesis | 90 | Loss of catalytic activity. | ||||
Sequence: H → Q | ||||||
Mutagenesis | 94 | Retains desampylating activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 98 | Loss of catalytic activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 101 | Loss of catalytic activity. | ||||
Sequence: D → E | ||||||
Mutagenesis | 115 | Retains desampylating activity. | ||||
Sequence: C → S |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000428938 | 1-139 | Desampylase | |||
Sequence: MTSSRLSLAADARDSILSHAREGAAGDPPAEVCGVLAGDSDARTVTAAHPVSNVAAEPRVAYELDPEETVSILEAIESAGDDAVGFYHSHPESDPVPSATDRERASWPGYVYLICSPDGRMTAHEWTGDEFRELSVAVE |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 6-139 | MPN | ||||
Sequence: LSLAADARDSILSHAREGAAGDPPAEVCGVLAGDSDARTVTAAHPVSNVAAEPRVAYELDPEETVSILEAIESAGDDAVGFYHSHPESDPVPSATDRERASWPGYVYLICSPDGRMTAHEWTGDEFRELSVAVE | ||||||
Motif | 88-101 | JAMM motif | ||||
Sequence: HSHPESDPVPSATD |
Sequence similarities
Belongs to the peptidase M67B family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length139
- Mass (Da)14,739
- Last updated2010-05-18 v1
- Checksum432D44455ADF0568
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001956 EMBL· GenBank· DDBJ | ADE04294.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AOHU01000045 EMBL· GenBank· DDBJ | ELY32652.1 EMBL· GenBank· DDBJ | Genomic DNA |