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P96717

- YWQE_BACSU

UniProt

P96717 - YWQE_BACSU

Protein

Tyrosine-protein phosphatase YwqE

Gene

ywqE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Dephosphorylates the phosphotyrosine-containing proteins YwqD, YwqF and Ssb.1 Publication

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

    Cofactori

    Manganese.

    Enzyme regulationi

    Inhibited by vanadate and sodium pyrophosphate. Not inhibited by sodium fluoride.

    pH dependencei

    Optimally active at alkaline pHs. Activity increases with increasing pHs.

    GO - Molecular functioni

    1. manganese ion binding Source: InterPro
    2. protein tyrosine phosphatase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese

    Enzyme and pathway databases

    BioCyciBSUB:BSU36240-MONOMER.
    SABIO-RKP96717.

    Protein family/group databases

    PptaseDBiP3D0505166.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein phosphatase YwqE (EC:3.1.3.48)
    Gene namesi
    Name:ywqE
    Ordered Locus Names:BSU36240
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU36240.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi3 – 31D → A: Large decrease in activity. 1 Publication
    Mutagenesisi5 – 51H → A: Large decrease in activity. 1 Publication
    Mutagenesisi7 – 71H → A: Large decrease in activity.
    Mutagenesisi42 – 421H → A: Large decrease in activity. 1 Publication
    Mutagenesisi136 – 1361H → A: Large decrease in activity. 1 Publication
    Mutagenesisi194 – 1941D → A: Large decrease in activity. 1 Publication
    Mutagenesisi196 – 1961H → A: Large decrease in activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 254254Tyrosine-protein phosphatase YwqEPRO_0000057893Add
    BLAST

    Proteomic databases

    PaxDbiP96717.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU36240.

    Structurei

    Secondary structure

    1
    254
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Beta strandi12 – 154
    Helixi19 – 3113
    Beta strandi36 – 383
    Beta strandi42 – 454
    Helixi52 – 6817
    Beta strandi74 – 763
    Beta strandi80 – 823
    Helixi87 – 926
    Helixi99 – 1013
    Beta strandi102 – 1087
    Helixi118 – 12710
    Beta strandi131 – 1355
    Helixi137 – 1393
    Helixi141 – 1455
    Helixi148 – 1558
    Beta strandi159 – 1635
    Helixi164 – 1685
    Turni169 – 1713
    Helixi173 – 18412
    Beta strandi190 – 1923
    Beta strandi197 – 2015
    Helixi205 – 21612
    Helixi219 – 23214

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3QY6X-ray1.80A1-254[»]
    3QY7X-ray1.62A1-254[»]
    ProteinModelPortaliP96717.
    SMRiP96717. Positions 1-237.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP96717.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CpsB/CapC family.Curated

    Phylogenomic databases

    eggNOGiCOG4464.
    HOGENOMiHOG000007624.
    KOiK01104.
    OMAiTPHTLNG.
    OrthoDBiEOG6PKFDD.
    PhylomeDBiP96717.

    Family and domain databases

    InterProiIPR016667. Caps_polysacc_synth_CpsB/CapC.
    IPR004013. PHP_C.
    IPR016195. Pol/histidinol_Pase-like.
    [Graphical view]
    PfamiPF02811. PHP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016557. Caps_synth_CpsB. 1 hit.
    SUPFAMiSSF89550. SSF89550. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P96717-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIDIHCHILP AMDDGAGDSA DSIEMARAAV RQGIRTIIAT PHHNNGVYKN    50
    EPAAVREAAD QLNKRLIKED IPLHVLPGQE IRIYGEVEQD LAKRQLLSLN 100
    DTKYILIEFP FDHVPRYAEQ LFYDLQLKGY IPVIAHPERN REIRENPSLL 150
    YHLVEKGAAS QITSGSLAGI FGKQLKAFSL RLVEANLIHF VASDAHNVKT 200
    RNFHTQEALY VLEKEFGSEL PYMLTENAEL LLRNQTIFRQ PPQPVKRRKL 250
    FGFF 254
    Length:254
    Mass (Da):28,958
    Last modified:May 1, 1997 - v1
    Checksum:iE2625AE51E0E9A94
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z92952 Genomic DNA. Translation: CAB07456.1.
    AL009126 Genomic DNA. Translation: CAB15641.1.
    PIRiH70066.
    RefSeqiNP_391505.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15641; CAB15641; BSU36240.
    GeneIDi936893.
    KEGGibsu:BSU36240.
    PATRICi18979268. VBIBacSub10457_3796.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z92952 Genomic DNA. Translation: CAB07456.1 .
    AL009126 Genomic DNA. Translation: CAB15641.1 .
    PIRi H70066.
    RefSeqi NP_391505.1. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QY6 X-ray 1.80 A 1-254 [» ]
    3QY7 X-ray 1.62 A 1-254 [» ]
    ProteinModelPortali P96717.
    SMRi P96717. Positions 1-237.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU36240.

    Protein family/group databases

    PptaseDBi P3D0505166.

    Proteomic databases

    PaxDbi P96717.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15641 ; CAB15641 ; BSU36240 .
    GeneIDi 936893.
    KEGGi bsu:BSU36240.
    PATRICi 18979268. VBIBacSub10457_3796.

    Organism-specific databases

    GenoListi BSU36240.

    Phylogenomic databases

    eggNOGi COG4464.
    HOGENOMi HOG000007624.
    KOi K01104.
    OMAi TPHTLNG.
    OrthoDBi EOG6PKFDD.
    PhylomeDBi P96717.

    Enzyme and pathway databases

    BioCyci BSUB:BSU36240-MONOMER.
    SABIO-RK P96717.

    Miscellaneous databases

    EvolutionaryTracei P96717.

    Family and domain databases

    InterProi IPR016667. Caps_polysacc_synth_CpsB/CapC.
    IPR004013. PHP_C.
    IPR016195. Pol/histidinol_Pase-like.
    [Graphical view ]
    Pfami PF02811. PHP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016557. Caps_synth_CpsB. 1 hit.
    SUPFAMi SSF89550. SSF89550. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
      Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
      Microbiology 143:3313-3328(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "In vitro characterization of the Bacillus subtilis protein tyrosine phosphatase YwqE."
      Mijakovic I., Musumeci L., Tautz L., Petranovic D., Edwards R.A., Jensen P.R., Mustelin T., Deutscher J., Bottini N.
      J. Bacteriol. 187:3384-3390(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF ASP-3; HIS-5; HIS-42; HIS-136; ASP-194 AND HIS-196.
    4. "Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine."
      Mijakovic I., Petranovic D., Macek B., Cepo T., Mann M., Davies J., Jensen P.R., Vujaklija D.
      Nucleic Acids Res. 34:1588-1596(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiYWQE_BACSU
    AccessioniPrimary (citable) accession number: P96717
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2003
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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

    External Data

    Dasty 3