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Protein

Low molecular weight protein-tyrosine-phosphatase YfkJ

Gene

yfkJ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Dephosphorylates the phosphotyrosine-containing proteins. Involved in ethanol stress resistance.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulationi

Efficiently inhibited by Cu2+ ion, Zn2+ ion 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

  1. KM=244 µM for p-nitrophenyl-phosphate (at 37 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei8 – 81Nucleophile
    Active sitei14 – 141
    Active sitei125 – 1251Proton donor

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    BioCyciBSUB:BSU07880-MONOMER.
    RETL1328306-WGS:GSTH-4023-MONOMER.
    SABIO-RKO35016.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Low molecular weight protein-tyrosine-phosphatase YfkJ (EC:3.1.3.48)
    Short name:
    LMPTP
    Gene namesi
    Name:yfkJ
    Ordered Locus Names:BSU07880
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570 Componenti: Chromosome

    Organism-specific databases

    GenoListiBSU07880.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi8 – 81C → S: Completely abolishes the tyrosine-phosphatase activity. 1 Publication
    Mutagenesisi14 – 141R → K: Completely abolishes the tyrosine-phosphatase activity. 1 Publication
    Mutagenesisi125 – 1251D → A: Completely abolishes the tyrosine-phosphatase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 156156Low molecular weight protein-tyrosine-phosphatase YfkJPRO_0000234659Add
    BLAST

    Proteomic databases

    PaxDbiO35016.

    Expressioni

    Inductioni

    By ethanol stress. Expression is sigma B-dependent.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100004383.

    Structurei

    Secondary structure

    1
    156
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 1312Combined sources
    Helixi14 – 2815Combined sources
    Turni32 – 343Combined sources
    Beta strandi35 – 439Combined sources
    Turni45 – 484Combined sources
    Helixi53 – 619Combined sources
    Helixi76 – 816Combined sources
    Beta strandi83 – 897Combined sources
    Helixi90 – 10011Combined sources
    Beta strandi108 – 1103Combined sources
    Helixi111 – 1144Combined sources
    Helixi126 – 1294Combined sources
    Helixi132 – 15322Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4ETMX-ray1.60A/B1-156[»]
    ProteinModelPortaliO35016.
    SMRiO35016. Positions 2-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0394.
    HOGENOMiHOG000273094.
    InParanoidiO35016.
    KOiK01104.
    OMAiGSWHIGK.
    OrthoDBiEOG6MH5JB.
    PhylomeDBiO35016.

    Family and domain databases

    InterProiIPR023485. Ptyr_pPase_SF.
    IPR017867. Tyr_phospatase_low_mol_wt.
    [Graphical view]
    PANTHERiPTHR11717:SF7. PTHR11717:SF7. 1 hit.
    PfamiPF01451. LMWPc. 1 hit.
    [Graphical view]
    PRINTSiPR00719. LMWPTPASE.
    SMARTiSM00226. LMWPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52788. SSF52788. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O35016-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MISVLFVCLG NICRSPMAEA IFRDLAAKKG LEGKIKADSA GIGGWHIGNP
    60 70 80 90 100
    PHEGTQEILR REGISFDGML ARQVSEQDLD DFDYIIAMDA ENIGSLRSMA
    110 120 130 140 150
    GFKNTSHIKR LLDYVEDSDL ADVPDPYYTG NFEEVCQLIK TGCEQLLASI

    QKEKQL
    Length:156
    Mass (Da):17,269
    Last modified:January 1, 1998 - v1
    Checksum:i7CDC8C4D6D0FD528
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL009126 Genomic DNA. Translation: CAB12617.1.
    D83967 Genomic DNA. Translation: BAA23400.1.
    PIRiE69808.
    RefSeqiNP_388669.1. NC_000964.3.
    WP_003243480.1. NZ_JNCM01000032.1.

    Genome annotation databases

    EnsemblBacteriaiCAB12617; CAB12617; BSU07880.
    GeneIDi939191.
    KEGGibsu:BSU07880.
    PATRICi18973226. VBIBacSub10457_0827.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL009126 Genomic DNA. Translation: CAB12617.1.
    D83967 Genomic DNA. Translation: BAA23400.1.
    PIRiE69808.
    RefSeqiNP_388669.1. NC_000964.3.
    WP_003243480.1. NZ_JNCM01000032.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4ETMX-ray1.60A/B1-156[»]
    ProteinModelPortaliO35016.
    SMRiO35016. Positions 2-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100004383.

    Proteomic databases

    PaxDbiO35016.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB12617; CAB12617; BSU07880.
    GeneIDi939191.
    KEGGibsu:BSU07880.
    PATRICi18973226. VBIBacSub10457_0827.

    Organism-specific databases

    GenoListiBSU07880.

    Phylogenomic databases

    eggNOGiCOG0394.
    HOGENOMiHOG000273094.
    InParanoidiO35016.
    KOiK01104.
    OMAiGSWHIGK.
    OrthoDBiEOG6MH5JB.
    PhylomeDBiO35016.

    Enzyme and pathway databases

    BioCyciBSUB:BSU07880-MONOMER.
    RETL1328306-WGS:GSTH-4023-MONOMER.
    SABIO-RKO35016.

    Family and domain databases

    InterProiIPR023485. Ptyr_pPase_SF.
    IPR017867. Tyr_phospatase_low_mol_wt.
    [Graphical view]
    PANTHERiPTHR11717:SF7. PTHR11717:SF7. 1 hit.
    PfamiPF01451. LMWPc. 1 hit.
    [Graphical view]
    PRINTSiPR00719. LMWPTPASE.
    SMARTiSM00226. LMWPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52788. SSF52788. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "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.
    2. "Nucleotide sequence analysis of B. subtilis cromosome in 74 degree region."
      Sekiguchi J., Yamamoto H., Uchiyama S., Fajar A.
      Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / AC327.
    3. "Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis."
      Musumeci L., Bongiorni C., Tautz L., Edwards R.A., Osterman A., Perego M., Mustelin T., Bottini N.
      J. Bacteriol. 187:4945-4956(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-8; ARG-14 AND ASP-125, CHARACTERIZATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: 168 / JH642.

    Entry informationi

    Entry nameiYFKJ_BACSU
    AccessioniPrimary (citable) accession number: O35016
    Secondary accession number(s): Q79EX9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2006
    Last sequence update: January 1, 1998
    Last modified: June 24, 2015
    This is version 90 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

    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 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.