Function and Biology Details
Reactions catalysed:
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Type III secreted modular tyrosine phosphatase, SptP/YopH
- Tyrosine-specific protein phosphatase, PTPase domain
- Small GTPase
- Protein-tyrosine phosphatase-like
- Virulence factor YopE, GAP domain
- Virulence factor YopE, GAP domain superfamily
- P-loop containing nucleoside triphosphate hydrolase
- Protein-tyrosine phosphatase, active site
4 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158897 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Secreted effector protein SptP
Molecule details ›
Chain: S
Length: 383 amino acids
Theoretical weight: 42.13 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli BL21
UniProt:
Sequence domains:
Structure domains:
Length: 383 amino acids
Theoretical weight: 42.13 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P74873 (Residues: 161-543; Coverage: 71%)
Sequence domains:
Structure domains:
Ras-related C3 botulinum toxin substrate 1
Molecule details ›
Chain: R
Length: 184 amino acids
Theoretical weight: 20.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
Length: 184 amino acids
Theoretical weight: 20.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical: P63000 (Residues: 1-184; Coverage: 96%)
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
