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P03772

- PP_LAMBD

UniProt

P03772 - PP_LAMBD

Protein

Serine/threonine-protein phosphatase

Gene
N/A
Organism
Enterobacteria phage lambda (Bacteriophage lambda)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Cofactori

    Binds 2 manganese ions per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi20 – 201Manganese 1
    Metal bindingi22 – 221Manganese 1
    Metal bindingi49 – 491Manganese 1
    Metal bindingi49 – 491Manganese 2
    Metal bindingi75 – 751Manganese 2
    Active sitei76 – 761Proton donorBy similarity
    Metal bindingi186 – 1861Manganese 2

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphoprotein phosphatase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase (EC:3.1.3.16)
    OrganismiEnterobacteria phage lambda (Bacteriophage lambda)
    Taxonomic identifieri10710 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesSiphoviridaeLambdalikevirus
    Virus hostiEscherichia coli [TaxID: 562]
    ProteomesiUP000001711: Genome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 221221Serine/threonine-protein phosphatasePRO_0000058912Add
    BLAST

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Plk4Q647022EBI-4478820,EBI-2552433From a different organism.

    Protein-protein interaction databases

    DIPiDIP-44028N.
    IntActiP03772. 3 interactions.
    MINTiMINT-4053809.

    Structurei

    Secondary structure

    1
    221
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Helixi9 – 113
    Beta strandi15 – 184
    Helixi25 – 3511
    Turni39 – 413
    Beta strandi43 – 464
    Beta strandi51 – 555
    Helixi57 – 615
    Helixi62 – 654
    Beta strandi69 – 713
    Helixi75 – 8410
    Helixi91 – 944
    Turni95 – 973
    Helixi98 – 1036
    Helixi106 – 11914
    Beta strandi124 – 1307
    Beta strandi133 – 1375
    Beta strandi144 – 1463
    Helixi155 – 1606
    Helixi163 – 1697
    Beta strandi179 – 1846
    Beta strandi193 – 1953
    Beta strandi198 – 2003
    Helixi205 – 2084
    Beta strandi213 – 2175

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G5BX-ray2.15A/B/C1-221[»]
    ProteinModelPortaliP03772.
    SMRiP03772. Positions 1-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03772.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family.Curated

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    SMARTiSM00156. PP2Ac. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P03772-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRYYEKIDGS KYRNIWVVGD LHGCYTNLMN KLDTIGFDNK KDLLISVGDL    50
    VDRGAENVEC LELITFPWFR AVRGNHEQMM IDGLSERGNV NHWLLNGGGW 100
    FFNLDYDKEI LAKALAHKAD ELPLIIELVS KDKKYVICHA DYPFDEYEFG 150
    KPVDHQQVIW NRERISNSQN GIVKEIKGAD TFIFGHTPAV KPLKFANQMY 200
    IDTGAVFCGN LTLIQVQGEG A 221
    Length:221
    Mass (Da):25,219
    Last modified:July 21, 1986 - v1
    Checksum:i5CE0E1A0F3BC5CB5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02459 Genomic DNA. Translation: AAA96594.1.
    PIRiG43011. Q1BP1L.
    RefSeqiNP_040641.1. NC_001416.1.

    Genome annotation databases

    GeneIDi2703476.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02459 Genomic DNA. Translation: AAA96594.1 .
    PIRi G43011. Q1BP1L.
    RefSeqi NP_040641.1. NC_001416.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G5B X-ray 2.15 A/B/C 1-221 [» ]
    ProteinModelPortali P03772.
    SMRi P03772. Positions 1-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-44028N.
    IntActi P03772. 3 interactions.
    MINTi MINT-4053809.

    Chemistry

    BindingDBi P03772.
    ChEMBLi CHEMBL3695.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2703476.

    Miscellaneous databases

    EvolutionaryTracei P03772.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    SMARTi SM00156. PP2Ac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Discovery of a protein phosphatase activity encoded in the genome of bacteriophage lambda. Probable identity with open reading frame 221."
      Cohen P.T.W., Cohen P.
      Biochem. J. 260:931-934(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    3. "Structure of the bacteriophage lambda Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes."
      Voegtli W.C., White D.J., Reiter N.J., Rusnak F., Rosenzweig A.C.
      Biochemistry 39:15365-15374(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS, COFACTOR.

    Entry informationi

    Entry nameiPP_LAMBD
    AccessioniPrimary (citable) accession number: P03772
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3