Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptidyl-tRNA hydrolase

Gene

pth

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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.

Catalytic activityi

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

GO - Molecular functioni

  • aminoacyl-tRNA hydrolase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciEcoCyc:EG10785-MONOMER.
ECOL316407:JW1195-MONOMER.
MetaCyc:EG10785-MONOMER.
BRENDAi3.1.1.29. 2026.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10785. pth.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi101G → D: Pth(ts) mutants synthesize thermosensitive PTH and die at 42 degrees Celsius from a defect in protein synthesis. 1
Mutagenesisi134R → H: Rap mutants do not support vegetative growth of bacteriophage lambda and die upon transcription of lambda DNA bar sites. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001877331 – 194Peptidyl-tRNA hydrolaseAdd BLAST194

Proteomic databases

EPDiP0A7D1.
PaxDbiP0A7D1.
PRIDEiP0A7D1.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4262870. 7 interactors.
DIPiDIP-35932N.
IntActiP0A7D1. 15 interactors.
MINTiMINT-1225563.
STRINGi511145.b1204.

Structurei

Secondary structure

1194
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Turni14 – 18Combined sources5
Helixi20 – 22Combined sources3
Helixi23 – 35Combined sources13
Beta strandi40 – 42Combined sources3
Helixi43 – 45Combined sources3
Beta strandi47 – 54Combined sources8
Beta strandi57 – 64Combined sources8
Helixi68 – 71Combined sources4
Helixi72 – 82Combined sources11
Helixi86 – 88Combined sources3
Beta strandi89 – 95Combined sources7
Beta strandi103 – 108Combined sources6
Helixi115 – 123Combined sources9
Beta strandi130 – 136Combined sources7
Helixi143 – 150Combined sources8
Helixi156 – 179Combined sources24
Helixi181 – 190Combined sources10
Turni191 – 193Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0A7D1.

Family & Domainsi

Sequence similaritiesi

Belongs to the PTH family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108ZPD. Bacteria.
COG0193. LUCA.
HOGENOMiHOG000004796.
InParanoidiP0A7D1.
KOiK01056.
OMAiRFYKILP.
PhylomeDBiP0A7D1.

Family and domain databases

CDDicd00462. PTH. 1 hit.
Gene3Di3.40.50.1470. 1 hit.
HAMAPiMF_00083. Pept_tRNA_hydro_bact. 1 hit.
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

        10         20         30         40         50
MTIKLIVGLA NPGAEYAATR HNAGAWFVDL LAERLRAPLR EEAKFFGYTS
60 70 80 90 100
RVTLGGEDVR LLVPTTFMNL SGKAVAAMAS FFRINPDEIL VAHDELDLPP
110 120 130 140 150
GVAKFKLGGG HGGHNGLKDI ISKLGNNPNF HRLRIGIGHP GDKNKVVGFV
160 170 180 190
LGKPPVSEQK LIDEAIDEAA RCTEMWFTDG LTKATNRLHA FKAQ
Length:194
Mass (Da):21,082
Last modified:June 7, 2005 - v1
Checksum:iA28A69A63F2DD530
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000152933.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74288; AAC74288; b1204.
BAA36062; BAA36062; BAA36062.
GeneIDi945765.
KEGGiecj:JW1195.
eco:b1204.
PATRICi32117660. VBIEscCol129921_1252.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000152933.1. NZ_LN832404.1.

3D structure databases

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

Protein-protein interaction databases

BioGridi4262870. 7 interactors.
DIPiDIP-35932N.
IntActiP0A7D1. 15 interactors.
MINTiMINT-1225563.
STRINGi511145.b1204.

Proteomic databases

EPDiP0A7D1.
PaxDbiP0A7D1.
PRIDEiP0A7D1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74288; AAC74288; b1204.
BAA36062; BAA36062; BAA36062.
GeneIDi945765.
KEGGiecj:JW1195.
eco:b1204.
PATRICi32117660. VBIEscCol129921_1252.

Organism-specific databases

EchoBASEiEB0778.
EcoGeneiEG10785. pth.

Phylogenomic databases

eggNOGiENOG4108ZPD. Bacteria.
COG0193. LUCA.
HOGENOMiHOG000004796.
InParanoidiP0A7D1.
KOiK01056.
OMAiRFYKILP.
PhylomeDBiP0A7D1.

Enzyme and pathway databases

BioCyciEcoCyc:EG10785-MONOMER.
ECOL316407:JW1195-MONOMER.
MetaCyc:EG10785-MONOMER.
BRENDAi3.1.1.29. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A7D1.
PROiP0A7D1.

Family and domain databases

CDDicd00462. PTH. 1 hit.
Gene3Di3.40.50.1470. 1 hit.
HAMAPiMF_00083. Pept_tRNA_hydro_bact. 1 hit.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 100 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

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 one 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.