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P0A7D1 (PTH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-tRNA hydrolase

Short name=PTH
EC=3.1.1.29
Gene names
Name:pth
Ordered Locus Names:b1204, JW1195
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00083

Catalytic activity

N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA. HAMAP-Rule MF_00083

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00083.

Sequence similarities

Belongs to the PTH family.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

prsP0A7171EBI-556507,EBI-906827

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194Peptidyl-tRNA hydrolase HAMAP-Rule MF_00083
PRO_0000187733

Experimental info

Mutagenesis1011G → D: Pth(ts) mutants synthesize thermosensitive PTH and die at 42 degrees Celsius from a defect in protein synthesis.
Mutagenesis1341R → H: Rap mutants do not support vegetative growth of bacteriophage lambda and die upon transcription of lambda DNA bar sites.

Secondary structure

.................................. 194
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7D1 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: A28A69A63F2DD530

FASTA19421,082
        10         20         30         40         50         60 
MTIKLIVGLA NPGAEYAATR HNAGAWFVDL LAERLRAPLR EEAKFFGYTS RVTLGGEDVR 

        70         80         90        100        110        120 
LLVPTTFMNL SGKAVAAMAS FFRINPDEIL VAHDELDLPP GVAKFKLGGG HGGHNGLKDI 

       130        140        150        160        170        180 
ISKLGNNPNF HRLRIGIGHP GDKNKVVGFV LGKPPVSEQK LIDEAIDEAA RCTEMWFTDG 

       190 
LTKATNRLHA FKAQ 

« Hide

References

« Hide 'large scale' references
[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]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61941 Genomic DNA. Translation: CAA43945.1.
U00096 Genomic DNA. Translation: AAC74288.1.
AP009048 Genomic DNA. Translation: BAA36062.1.
PIRS16753.
RefSeqNP_415722.1. NC_000913.3.
YP_489471.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PTHX-ray1.20A2-194[»]
3VJRX-ray2.40A/C1-194[»]
ProteinModelPortalP0A7D1.
SMRP0A7D1. Positions 2-194.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35932N.
IntActP0A7D1. 15 interactions.
MINTMINT-1225563.
STRING511145.b1204.

Proteomic databases

PaxDbP0A7D1.
PRIDEP0A7D1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74288; AAC74288; b1204.
BAA36062; BAA36062; BAA36062.
GeneID12933876.
945765.
KEGGecj:Y75_p1176.
eco:b1204.
PATRIC32117660. VBIEscCol129921_1252.

Organism-specific databases

EchoBASEEB0778.
EcoGeneEG10785. pth.

Phylogenomic databases

eggNOGCOG0193.
HOGENOMHOG000004796.
KOK01056.
OMAIKFKTGG.
OrthoDBEOG6C5RTR.
PhylomeDBP0A7D1.
ProtClustDBPRK05426.

Enzyme and pathway databases

BioCycEcoCyc:EG10785-MONOMER.
ECOL316407:JW1195-MONOMER.
MetaCyc:EG10785-MONOMER.

Gene expression databases

GenevestigatorP0A7D1.

Family and domain databases

Gene3D3.40.50.1470. 1 hit.
HAMAPMF_00083. Pept_tRNA_hydro_bact.
InterProIPR001328. Pept_tRNA_hydro.
IPR018171. Pept_tRNA_hydro_CS.
[Graphical view]
PANTHERPTHR17224. PTHR17224. 1 hit.
PfamPF01195. Pept_tRNA_hydro. 1 hit.
[Graphical view]
SUPFAMSSF53178. SSF53178. 1 hit.
TIGRFAMsTIGR00447. pth. 1 hit.
PROSITEPS01195. PEPT_TRNA_HYDROL_1. 1 hit.
PS01196. PEPT_TRNA_HYDROL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7D1.
PROP0A7D1.

Entry information

Entry namePTH_ECOLI
AccessionPrimary (citable) accession number: P0A7D1
Secondary accession number(s): P23932
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 16, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

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