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Protein

Protein-arginine-phosphatase

Gene

ywlE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

A [protein]-N(omega)-phospho-L-arginine + H2O = a [protein]-L-arginine + phosphate.1 Publication

Enzyme regulationi

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.1 Publication

Kineticsi

kcat is 0.010 sec(-1) with pNPP as substrate (at 37 degrees Celsius and pH 5.5) (PubMed:15995210) and 0.13 sec(-1) with pNPP as substrate (at 40 degrees Celsius and pH 8.0) (PubMed:23770242). pNPP is a phospho-tyrosine mimicking compound.2 Publications

Manual assertion based on experiment ini

  1. KM=0.157 mM for p-nitrophenyl-phosphate (at 37 degrees Celsius and pH 5.5)3 Publications
  2. KM=28 mM for p-nitrophenyl-phosphate (at 55 degrees Celsius)3 Publications
  3. KM=61.41 mM for p-nitrophenyl-phosphate (at 40 degrees Celsius and pH 8.0)3 Publications

    pH dependencei

    Optimum pH is 5.5 with pNPP as substrate.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei7Nucleophile1 Publication1
    Sitei11Important for substrate discrimination1
    Active sitei118Proton donor/acceptor1 Publication1

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    BioCyciBSUB:BSU36930-MONOMER.
    BRENDAi3.1.3.48. 658.
    SABIO-RKP39155.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-arginine-phosphatase (EC:3.9.1.21 Publication)
    Short name:
    PAP
    Alternative name(s):
    Phosphoarginine phosphatase
    Gene namesi
    Name:ywlE
    Ordered Locus Names:BSU36930
    ORF Names:ipc-31d
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    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 and 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).4 Publications

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi7C → S: Complete loss of phosphatase activity. 1 Publication1
    Mutagenesisi11T → I: 18-fold reduction in p-Arg phosphatase activity and 22-fold increase in p-Tyr phosphatase activity. 1 Publication1
    Mutagenesisi11T → V: 18-fold reduction in p-Arg phosphatase activity and 11-fold increase in p-Tyr phosphatase activity. 1 Publication1
    Mutagenesisi13R → K: Completely loss of phosphatase activity. 1 Publication1
    Mutagenesisi118D → A: Completely loss of phosphatase activity. 2 Publications1
    Mutagenesisi120F → A: 60-fold reduction in p-Arg phosphatase activity and 4-fold reduction in p-Tyr phosphatase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000465791 – 150Protein-arginine-phosphataseAdd BLAST150

    Proteomic databases

    PaxDbiP39155.

    Expressioni

    Inductioni

    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.1 Publication

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-7148489.
    STRINGi224308.Bsubs1_010100019966.

    Structurei

    Secondary structure

    1150
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi1 – 12Combined sources12
    Helixi13 – 28Combined sources16
    Beta strandi32 – 38Combined sources7
    Helixi49 – 57Combined sources9
    Helixi71 – 76Combined sources6
    Beta strandi78 – 84Combined sources7
    Helixi85 – 94Combined sources10
    Helixi96 – 101Combined sources6
    Beta strandi102 – 104Combined sources3
    Helixi105 – 110Combined sources6
    Beta strandi111 – 113Combined sources3
    Helixi124 – 145Combined sources22
    Turni146 – 148Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1ZGGNMR-A1-150[»]
    4ETIX-ray1.80A1-150[»]
    4ETNX-ray1.10A1-150[»]
    4KK3X-ray1.70A1-150[»]
    4KK4X-ray1.80A1-150[»]
    ProteinModelPortaliP39155.
    SMRiP39155.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39155.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni8 – 13Substrate binding6

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4107WAU. Bacteria.
    COG0394. LUCA.
    HOGENOMiHOG000273091.
    InParanoidiP39155.
    KOiK20201.
    OMAiSIDIYKQ.
    PhylomeDBiP39155.

    Family and domain databases

    CDDicd00115. LMWPc. 1 hit.
    InterProiIPR023485. Ptyr_pPase_SF.
    IPR017867. Tyr_phospatase_low_mol_wt.
    [Graphical view]
    PANTHERiPTHR11717:SF14. PTHR11717:SF14. 1 hit.
    PfamiPF01451. LMWPc. 1 hit.
    [Graphical view]
    PRINTSiPR00719. LMWPTPASE.
    SMARTiSM00226. LMWPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52788. SSF52788. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P39155-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDIIFVCTGN TCRSPMAEAL FKSIAEREGL NVNVRSAGVF ASPNGKATPH
    60 70 80 90 100
    AVEALFEKHI ALNHVSSPLT EELMESADLV LAMTHQHKQI IASQFGRYRD
    110 120 130 140 150
    KVFTLKEYVT GSHGDVLDPF GGSIDIYKQT RDELEELLRQ LAKQLKKDRR
    Length:150
    Mass (Da):16,785
    Last modified:February 1, 1995 - v1
    Checksum:iE1BD5EA5231DED2C
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z38002 Genomic DNA. Translation: CAA86107.1.
    AL009126 Genomic DNA. Translation: CAB15710.1.
    PIRiI40479. S49360.
    RefSeqiNP_391574.1. NC_000964.3.
    WP_003227664.1. NZ_JNCM01000034.1.

    Genome annotation databases

    EnsemblBacteriaiCAB15710; CAB15710; BSU36930.
    GeneIDi937021.
    KEGGibsu:BSU36930.
    PATRICi18979420. VBIBacSub10457_3872.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z38002 Genomic DNA. Translation: CAA86107.1.
    AL009126 Genomic DNA. Translation: CAB15710.1.
    PIRiI40479. S49360.
    RefSeqiNP_391574.1. NC_000964.3.
    WP_003227664.1. NZ_JNCM01000034.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1ZGGNMR-A1-150[»]
    4ETIX-ray1.80A1-150[»]
    4ETNX-ray1.10A1-150[»]
    4KK3X-ray1.70A1-150[»]
    4KK4X-ray1.80A1-150[»]
    ProteinModelPortaliP39155.
    SMRiP39155.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    MINTiMINT-7148489.
    STRINGi224308.Bsubs1_010100019966.

    Proteomic databases

    PaxDbiP39155.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB15710; CAB15710; BSU36930.
    GeneIDi937021.
    KEGGibsu:BSU36930.
    PATRICi18979420. VBIBacSub10457_3872.

    Phylogenomic databases

    eggNOGiENOG4107WAU. Bacteria.
    COG0394. LUCA.
    HOGENOMiHOG000273091.
    InParanoidiP39155.
    KOiK20201.
    OMAiSIDIYKQ.
    PhylomeDBiP39155.

    Enzyme and pathway databases

    BioCyciBSUB:BSU36930-MONOMER.
    BRENDAi3.1.3.48. 658.
    SABIO-RKP39155.

    Miscellaneous databases

    EvolutionaryTraceiP39155.

    Family and domain databases

    CDDicd00115. LMWPc. 1 hit.
    InterProiIPR023485. Ptyr_pPase_SF.
    IPR017867. Tyr_phospatase_low_mol_wt.
    [Graphical view]
    PANTHERiPTHR11717:SF14. PTHR11717:SF14. 1 hit.
    PfamiPF01451. LMWPc. 1 hit.
    [Graphical view]
    PRINTSiPR00719. LMWPTPASE.
    SMARTiSM00226. LMWPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52788. SSF52788. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPAP_BACSU
    AccessioniPrimary (citable) accession number: P39155
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: November 2, 2016
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to be a protein-tyrosine-phosphatase (PubMed:15995210). Was later shown to function as an arginine phosphatase in vivo and in vitro (PubMed:22517742 and PubMed:23770242).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.