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P0A7D1

- PTH_ECOLI

UniProt

P0A7D1 - PTH_ECOLI

Protein

Peptidyl-tRNA hydrolase

Gene

pth

Organism
Escherichia coli (strain K12)
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 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis. Involved in lambda inhibition of host protein synthesis. PTH activity may, directly or indirectly, be the target for lambda bar RNA leading to rap cell death.

    Catalytic activityi

    N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA.UniRule annotation

    GO - Molecular functioni

    1. aminoacyl-tRNA hydrolase activity Source: EcoCyc

    GO - Biological processi

    1. misfolded or incompletely synthesized protein catabolic process Source: EcoCyc

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10785-MONOMER.
    ECOL316407:JW1195-MONOMER.
    MetaCyc:EG10785-MONOMER.
    SABIO-RKP0A7D1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peptidyl-tRNA hydrolaseUniRule annotation (EC:3.1.1.29UniRule annotation)
    Short name:
    PTHUniRule annotation
    Gene namesi
    Name:pthUniRule annotation
    Ordered Locus Names:b1204, JW1195
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10785. pth.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi101 – 1011G → D: Pth(ts) mutants synthesize thermosensitive PTH and die at 42 degrees Celsius from a defect in protein synthesis.
    Mutagenesisi134 – 1341R → H: Rap mutants do not support vegetative growth of bacteriophage lambda and die upon transcription of lambda DNA bar sites.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 194194Peptidyl-tRNA hydrolasePRO_0000187733Add
    BLAST

    Proteomic databases

    PaxDbiP0A7D1.
    PRIDEiP0A7D1.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7D1.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    prsP0A7171EBI-556507,EBI-906827

    Protein-protein interaction databases

    DIPiDIP-35932N.
    IntActiP0A7D1. 15 interactions.
    MINTiMINT-1225563.
    STRINGi511145.b1204.

    Structurei

    Secondary structure

    1
    194
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84
    Turni14 – 185
    Helixi20 – 223
    Helixi23 – 3513
    Beta strandi40 – 423
    Helixi43 – 453
    Beta strandi47 – 548
    Beta strandi57 – 648
    Helixi68 – 714
    Helixi72 – 8211
    Helixi86 – 883
    Beta strandi89 – 957
    Beta strandi103 – 1086
    Helixi115 – 1239
    Beta strandi130 – 1367
    Helixi143 – 1508
    Helixi156 – 17924
    Helixi181 – 19010
    Turni191 – 1933

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2PTHX-ray1.20A2-194[»]
    3VJRX-ray2.40A/C1-194[»]
    ProteinModelPortaliP0A7D1.
    SMRiP0A7D1. Positions 2-194.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7D1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PTH family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0193.
    HOGENOMiHOG000004796.
    KOiK01056.
    OMAiAMHRLHS.
    OrthoDBiEOG6C5RTR.
    PhylomeDBiP0A7D1.

    Family and domain databases

    Gene3Di3.40.50.1470. 1 hit.
    HAMAPiMF_00083. Pept_tRNA_hydro_bact.
    InterProiIPR001328. Pept_tRNA_hydro.
    IPR018171. Pept_tRNA_hydro_CS.
    [Graphical view]
    PANTHERiPTHR17224. PTHR17224. 1 hit.
    PfamiPF01195. Pept_tRNA_hydro. 1 hit.
    [Graphical view]
    SUPFAMiSSF53178. SSF53178. 1 hit.
    TIGRFAMsiTIGR00447. pth. 1 hit.
    PROSITEiPS01195. PEPT_TRNA_HYDROL_1. 1 hit.
    PS01196. PEPT_TRNA_HYDROL_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A7D1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTIKLIVGLA NPGAEYAATR HNAGAWFVDL LAERLRAPLR EEAKFFGYTS    50
    RVTLGGEDVR LLVPTTFMNL SGKAVAAMAS FFRINPDEIL VAHDELDLPP 100
    GVAKFKLGGG HGGHNGLKDI ISKLGNNPNF HRLRIGIGHP GDKNKVVGFV 150
    LGKPPVSEQK LIDEAIDEAA RCTEMWFTDG LTKATNRLHA FKAQ 194
    Length:194
    Mass (Da):21,082
    Last modified:June 7, 2005 - v1
    Checksum:iA28A69A63F2DD530
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61941 Genomic DNA. Translation: CAA43945.1.
    U00096 Genomic DNA. Translation: AAC74288.1.
    AP009048 Genomic DNA. Translation: BAA36062.1.
    PIRiS16753.
    RefSeqiNP_415722.1. NC_000913.3.
    YP_489471.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74288; AAC74288; b1204.
    BAA36062; BAA36062; BAA36062.
    GeneIDi12933876.
    945765.
    KEGGiecj:Y75_p1176.
    eco:b1204.
    PATRICi32117660. VBIEscCol129921_1252.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61941 Genomic DNA. Translation: CAA43945.1 .
    U00096 Genomic DNA. Translation: AAC74288.1 .
    AP009048 Genomic DNA. Translation: BAA36062.1 .
    PIRi S16753.
    RefSeqi NP_415722.1. NC_000913.3.
    YP_489471.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PTH X-ray 1.20 A 2-194 [» ]
    3VJR X-ray 2.40 A/C 1-194 [» ]
    ProteinModelPortali P0A7D1.
    SMRi P0A7D1. Positions 2-194.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35932N.
    IntActi P0A7D1. 15 interactions.
    MINTi MINT-1225563.
    STRINGi 511145.b1204.

    Proteomic databases

    PaxDbi P0A7D1.
    PRIDEi P0A7D1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74288 ; AAC74288 ; b1204 .
    BAA36062 ; BAA36062 ; BAA36062 .
    GeneIDi 12933876.
    945765.
    KEGGi ecj:Y75_p1176.
    eco:b1204.
    PATRICi 32117660. VBIEscCol129921_1252.

    Organism-specific databases

    EchoBASEi EB0778.
    EcoGenei EG10785. pth.

    Phylogenomic databases

    eggNOGi COG0193.
    HOGENOMi HOG000004796.
    KOi K01056.
    OMAi AMHRLHS.
    OrthoDBi EOG6C5RTR.
    PhylomeDBi P0A7D1.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10785-MONOMER.
    ECOL316407:JW1195-MONOMER.
    MetaCyc:EG10785-MONOMER.
    SABIO-RK P0A7D1.

    Miscellaneous databases

    EvolutionaryTracei P0A7D1.
    PROi P0A7D1.

    Gene expression databases

    Genevestigatori P0A7D1.

    Family and domain databases

    Gene3Di 3.40.50.1470. 1 hit.
    HAMAPi MF_00083. Pept_tRNA_hydro_bact.
    InterProi IPR001328. Pept_tRNA_hydro.
    IPR018171. Pept_tRNA_hydro_CS.
    [Graphical view ]
    PANTHERi PTHR17224. PTHR17224. 1 hit.
    Pfami PF01195. Pept_tRNA_hydro. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53178. SSF53178. 1 hit.
    TIGRFAMsi TIGR00447. pth. 1 hit.
    PROSITEi PS01195. PEPT_TRNA_HYDROL_1. 1 hit.
    PS01196. PEPT_TRNA_HYDROL_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Peptidyl-tRNA hydrolase is involved in lambda inhibition of host protein synthesis."
      Garcia-Villegas M.R., de la Vega F.M., Galindo J.M., Segura M., Buckingham R.H., Guarneros G.
      EMBO J. 10:3549-3555(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17.
      Strain: K12.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Crystallization and preliminary X-ray analysis of Escherichia coli peptidyl-tRNA hydrolase."
      Schmitt E., Fromant M., Plateau P., Mechulam Y., Blanquet S.
      Proteins 28:135-136(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION.
    6. "Crystal structure at 1.2-A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase."
      Schmitt E., Mechulam Y., Fromant M., Plateau P., Blanquet S.
      EMBO J. 16:4760-4769(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).

    Entry informationi

    Entry nameiPTH_ECOLI
    AccessioniPrimary (citable) accession number: P0A7D1
    Secondary accession number(s): P23932
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    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, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    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