P39155 · PAP_BACSU
- ProteinProtein-arginine-phosphatase
- GeneywlE
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids150 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the specific dephosphorylation of phosphoarginine residues in a large number of proteins. Counteracts the protein arginine kinase McsB in vivo. Can dephosphorylate CtsR-P; thus, can restore the DNA-binding ability of the CtsR repressor by reversing the McsB-mediated phosphorylation. Is the only active pArg phosphatase present in B.subtilis. Exhibits almost no activity against pSer, pThr, or pTyr peptides. Appears to play a role in B.subtilis stress resistance. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity.
Catalytic activity
- H2O + N(omega)-phospho-L-arginyl-[protein] = L-arginyl-[protein] + phosphate
Activity regulation
Efficiently inhibited by Cu2+ ion, Zn2+ ion, sodium pyrophosphate and N-ethylmaleimide, while the addition of Mg2+, Ca2+ or Fe3+ ions has minimal effect. Inhibited in a competitive manner by vanadate.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.157 mM | p-nitrophenyl-phosphate | 5.5 | 37 | |||
28 mM | p-nitrophenyl-phosphate | 55 | ||||
61.41 mM | p-nitrophenyl-phosphate | 8.0 | 40 |
kcat is 0.010 sec-1 with pNPP as substrate (at 37 degrees Celsius and pH 5.5) (PubMed:15995210).
kcat is 0.13 sec-1 with pNPP as substrate (at 40 degrees Celsius and pH 8.0) (PubMed:23770242).
pNPP is a phosphotyrosine mimicking compound.
kcat is 0.13 sec-1 with pNPP as substrate (at 40 degrees Celsius and pH 8.0) (PubMed:23770242).
pNPP is a phosphotyrosine mimicking compound.
pH Dependence
Optimum pH is 5.5 with pNPP as substrate.
Features
Showing features for active site, binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 7 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 8-13 | substrate | ||||
Sequence: TGNTCR | ||||||
Site | 11 | Important for substrate discrimination | ||||
Sequence: T | ||||||
Active site | 13 | |||||
Sequence: R | ||||||
Active site | 118 | Proton donor/acceptor | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | protein arginine phosphatase activity | |
Molecular Function | protein tyrosine phosphatase activity |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein-arginine-phosphatase
- EC number
- Short namesPAP
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionP39155
Proteomes
Phenotypes & Variants
Disruption phenotype
Cellular protein arginine phosphorylation is only detectable in a ywlE mutant and not in the wild-type strain, and global gene expression is significantly impacted in the mutant strain (PubMed:22517742, PubMed:24263382).
Cells lacking this gene are impaired in dephosphorylating McsB-P (PubMed:23770242).
They also show a reduced resistance to ethanol stress (PubMed:15995210).
Cells lacking this gene are impaired in dephosphorylating McsB-P (PubMed:23770242).
They also show a reduced resistance to ethanol stress (PubMed:15995210).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 7 | Complete loss of phosphatase activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 11 | 18-fold reduction in p-Arg phosphatase activity and 22-fold increase in p-Tyr phosphatase activity. | ||||
Sequence: T → I | ||||||
Mutagenesis | 11 | 18-fold reduction in p-Arg phosphatase activity and 11-fold increase in p-Tyr phosphatase activity. | ||||
Sequence: T → V | ||||||
Mutagenesis | 13 | Completely loss of phosphatase activity. | ||||
Sequence: R → K | ||||||
Mutagenesis | 118 | Completely loss of phosphatase activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 120 | 60-fold reduction in p-Arg phosphatase activity and 4-fold reduction in p-Tyr phosphatase activity. | ||||
Sequence: F → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000046579 | 1-150 | Protein-arginine-phosphatase | |||
Sequence: MDIIFVCTGNTCRSPMAEALFKSIAEREGLNVNVRSAGVFASPNGKATPHAVEALFEKHIALNHVSSPLTEELMESADLVLAMTHQHKQIIASQFGRYRDKVFTLKEYVTGSHGDVLDPFGGSIDIYKQTRDELEELLRQLAKQLKKDRR |
Proteomic databases
Expression
Induction
Expression is up-regulated in the exponential phase of growth, followed by a significant and gradual reduction in the stationary/sporulation phase. Is not up-regulated during ethanol stress.
Structure
Sequence
- Sequence statusComplete
- Length150
- Mass (Da)16,785
- Last updated1995-02-01 v1
- ChecksumE1BD5EA5231DED2C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z38002 EMBL· GenBank· DDBJ | CAA86107.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009126 EMBL· GenBank· DDBJ | CAB15710.1 EMBL· GenBank· DDBJ | Genomic DNA |