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P0A7D1

- PTH_ECOLI

UniProt

P0A7D1 - PTH_ECOLI

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Protein

Peptidyl-tRNA hydrolase

Gene
pth, b1204, JW1195
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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.UniRule annotation

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
Complete GO annotation...

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 hydrolase (EC:3.1.1.29)
Short name:
PTH
Gene namesi
Name:pth
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

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

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 hydrolaseUniRule annotationPRO_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.

Miscellaneous databases

EvolutionaryTraceiP0A7D1.

Family & Domainsi

Sequence similaritiesi

Belongs to the PTH family.

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 83 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

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