Q8Y678 · STP1_LISMO
- ProteinSerine/threonine phosphatase stp
- Genestp
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids252 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein phosphatase that dephosphorylates EF-Tu.
Catalytic activity
- H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Cofactor
Note: Binds 2 manganese ions per subunit.
Activity regulation
Activity not affected by inhibitors of phosphatases of the PPP family such as okadaic acid and cypermethrin, or by inhibitors of phosphatases of the PTP family such as sodium orthovanadate.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
3.77 μM | MBP | |||||
0.62 μM | EF-Tu |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
120.48 pmol/min/ug | toward MBP | ||||
2.94 pmol/min/ug | toward EF-Tu |
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | membrane | |
Molecular Function | metal ion binding | |
Molecular Function | myosin phosphatase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine phosphatase stp
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Listeriaceae > Listeria
Accessions
- Primary accessionQ8Y678
Proteomes
Phenotypes & Variants
Disruption phenotype
The stp-disrupted strain is 4 times less virulent than the wild strain, demonstrating that stp is required for full virulence of L.monocytogenes in BALB/c mice.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000363063 | 1-252 | Serine/threonine phosphatase stp | |||
Sequence: MHAEFRTDRGRIRHHNEDNGGVFENKDNQPIVIVADGMGGHRAGDVASEMAVRLLSDAWKETTALLTAEEIETWLRKTIQEVNKEIVLYAESEMDLNGMGTTLVAAIMAQSQVVIANVGDSRGYLLQNHVLRQLTEDHSLVHELLRTGEISKEDAMNHPRKNILLRALGVEGKVEVDTFVVPFQTSDTLLLCSDGLTNMVPETEMEEILKSKRTLSEKADVFITKANSYGGEDNITVLLVERDLTQKGRDAS |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Basic and acidic residues | ||||
Sequence: MHAEFRTDRGRIRHHNEDNGGV | ||||||
Region | 1-23 | Disordered | ||||
Sequence: MHAEFRTDRGRIRHHNEDNGGVF | ||||||
Domain | 2-242 | PPM-type phosphatase | ||||
Sequence: HAEFRTDRGRIRHHNEDNGGVFENKDNQPIVIVADGMGGHRAGDVASEMAVRLLSDAWKETTALLTAEEIETWLRKTIQEVNKEIVLYAESEMDLNGMGTTLVAAIMAQSQVVIANVGDSRGYLLQNHVLRQLTEDHSLVHELLRTGEISKEDAMNHPRKNILLRALGVEGKVEVDTFVVPFQTSDTLLLCSDGLTNMVPETEMEEILKSKRTLSEKADVFITKANSYGGEDNITVLLVER |
Sequence similarities
Belongs to the PP2C family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length252
- Mass (Da)28,026
- Last updated2002-03-01 v1
- Checksum47EE5DA232A43338
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Basic and acidic residues | ||||
Sequence: MHAEFRTDRGRIRHHNEDNGGV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL591981 EMBL· GenBank· DDBJ | CAC99899.1 EMBL· GenBank· DDBJ | Genomic DNA |