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Protein

Protein-arginine-phosphatase

Gene

ywlE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -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

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

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

    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

    Keywordsi

    Molecular functionHydrolase, 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
    PRIDEiP39155

    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

    MINTiP39155
    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
    OMAiIFVCTGN
    PhylomeDBiP39155

    Family and domain databases

    InterProiView protein in InterPro
    IPR023485 Ptyr_pPase
    IPR036196 Ptyr_pPase_sf
    IPR017867 Tyr_phospatase_low_mol_wt
    PfamiView protein in Pfam
    PF01451 LMWPc, 1 hit
    PRINTSiPR00719 LMWPTPASE
    SMARTiView protein in SMART
    SM00226 LMWPc, 1 hit
    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
    PATRICifig|224308.179.peg.4000

    Entry informationi

    Entry nameiPAP_BACSU
    AccessioniPrimary (citable) accession number: P39155
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: May 23, 2018
    This is version 132 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

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