Peptidyl-tRNA hydrolase (P0A7D1)

Identification
Name:Peptidyl-tRNA hydrolase
Synonyms:
  • PTH
Gene Name:pth
Enzyme Class:
Biological Properties
General Function:Involved in aminoacyl-tRNA hydrolase activity
Specific 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
Cellular Location:Cytoplasm
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
KEGG Reactions:
1.0N-Substituted aminoacyl-tRNA+1.0Thumb ↔ 1.0N-Substituted amino acid+1.0tRNA
1.0N-Substituted aminoacyl-tRNA + 1.0Water ↔ 1.0N-Substituted amino acid + 1.0tRNA
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00494WaterMetaboCard
GO Classification:
Function
aminoacyl-tRNA hydrolase activity
carboxylesterase activity
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
Process
biosynthetic process
cellular macromolecule biosynthetic process
macromolecule biosynthetic process
metabolic process
translation
Gene Properties
Blattner:b1204
Gene OrientationCounterclockwise
Centisome Percentage:27.10
Left Sequence End1257152
Right Sequence End1257736
Gene Sequence:
>585 bp
ATGTTTGGCTATCGCAGTAACGTGCCAAAAGTGCGCTTAACCACAGACCGACTGGTCGTG
CGTCTGGTGCATGATCGTGATGCCTGGCGTCTTGCGGATTATTACGCAGAGAATCGCCAT
TTCCTCAAGCCCTGGGAGCCAGTGCGCGACGAAAGCCACTGTTATCCATCAGGCTGGCAG
GCCAGGCTGGGGATGATTAACGAATTTCATAAACAAGGTTCAGCTTTCTACTTTGGCTTA
TTCGACCCGGACGAAAAAGAGATTATTGGCGTTGCCAATTTTTCCAATGTTGTTCGTGGC
TCTTTTCATGCCTGCTATCTCGGTTATTCGATTGGGCAAAAATGGCAGGGCAAAGGACTC
ATGTTTGAAGCCCTGACCGCAGCCATTCGTTATATGCAGCGCACCCAACATATTCATCGC
ATTATGGCTAATTATATGCCGCACAATAAACGCAGCGGTGATTTACTGGCGCGACTGGGT
TTTGAAAAAGAAGGCTATGCGAAAGACTATCTGTTGATTGATGGACAATGGCGCGATCAC
GTACTGACGGCATTAACTACCCCAGACTGGACGCCCGGCCGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:194
Protein Molecular Weight:21082
Protein Theoretical pI:10
PDB File:2PTH
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Peptidyl-tRNA hydrolase
MTIKLIVGLANPGAEYAATRHNAGAWFVDLLAERLRAPLREEAKFFGYTSRVTLGGEDVR
LLVPTTFMNLSGKAVAAMASFFRINPDEILVAHDELDLPPGVAKFKLGGGHGGHNGLKDI
ISKLGNNPNFHRLRIGIGHPGDKNKVVGFVLGKPPVSEQKLIDEAIDEAARCTEMWFTDG
LTKATNRLHAFKAQ
References
External Links:
ResourceLink
Uniprot ID:P0A7D1
Uniprot Name:PTH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1651524
PDB ID:2PTH
Ecogene ID:EG10785
Ecocyc:EG10785
ColiBase:b1204
Kegg Gene:b1204
EchoBASE ID:EB0778
CCDB:PTH_ECOLI
BacMap:16129167
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Garcia-Villegas, M. R., De La Vega, F. M., Galindo, J. M., Segura, M., Buckingham, R. H., Guarneros, G. (1991). "Peptidyl-tRNA hydrolase is involved in lambda inhibition of host protein synthesis." EMBO J 10:3549-3555. Pubmed: 1833189
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • 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., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "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." DNA Res 3:137-155. Pubmed: 8905232
  • Schmitt, E., Fromant, M., Plateau, P., Mechulam, Y., Blanquet, S. (1997). "Crystallization and preliminary X-ray analysis of Escherichia coli peptidyl-tRNA hydrolase." Proteins 28:135-136. Pubmed: 9144799
  • Schmitt, E., Mechulam, Y., Fromant, M., Plateau, P., Blanquet, S. (1997). "Crystal structure at 1.2 A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase." EMBO J 16:4760-4769. Pubmed: 9303320