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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0313 IGR0315 IGR0310 IGR0317 IGR0318 IGR0312 IGR0311 IGR0319 IGR0316 IGR0314 NG0378 NG0381 ppiB, - NG0376 pth, - NG0379 ftsJ,rrmJ, - NG0383 pgm, - NG0375 NG0377 ftsH,hflB, - NG0382 NG0384 glnQ, - NG0374 hemB, - NG0385 NG0378 NG0381 ppiB, - NG0376 pth, - NG0379 ftsJ,rrmJ, - NG0383 pgm, - NG0375 NG0377 ftsH,hflB, - NG0382 NG0384 glnQ, - NG0374 hemB, - NG0385 NG0378 ppiB, - NG0376 pth, - NG0379 ftsJ,rrmJ, - NG0383 pgm, - NG0375 NG0377 ftsH,hflB, - NG0382 NG0380 NG0381 NG0380 NG0384 glnQ, - NG0374 hemB, - NG0385
* Calculated from Protein Sequence

Gene ID: NG0379

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
pth  

Definition:
peptidyl-tRNA hydrolase (aminoacyl-tRNA hydrolase)

Gene Start:
373736

Gene Stop:
373161

Gene Length:
576

Molecular Weight*:
21430

pI*:
10.00

Net Charge*:
6.39

EC:
3.1.1.29  

Functional Class:
Translation; Amino acyl tRNA synthetases and tRNA modification  

Pathway: pathway table

Secondary Evidence:
Schmitt,E., Mechulam,Y., Fromant,M., Plateau,P. and Blanquet,S. 1997.
Crystal structure at 1.2 A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase.
EMBO J. 16 (15): 4760-4769.
Medline: 97447580.

Garcia-Villegas,M.R., De La Vega,F.M., Galindo,J.M., Segura,M., Buckingham,R.H. and Guarneros,G.
Peptidyl-tRNA hydrolase is involved in lambda inhibition of host protein synthesis.
EMBO J. 10 (11): 3549-3555.
Medline: 92007806.

Menez J, Buckingham RH, Zamaroczy Md M, Campelli CK.
Peptidyl-tRNA hydrolase in Bacillus subtilis, encoded
by spoVC, is essential to vegetative growth,whereas the homologous enzyme in Saccharomyces cerevisiae is dispensable.
Mol Microbiol. 2002 Jul;45(1):123-9.
PMID: 12100553

Bonin PD, Choi GH, Trepod CM, Mott JE, Lyle SB, Cialdella JI, Sarver RW, Marshall VP, Erickson LA.
Expression, purification, and characterization of peptidyl-tRNA hydrolase from Staphylococcus aureus.
Protein Expr Purif. 2002 Feb;24(1):123-30.
PMID: 11812233

Menez J, Remy E, Buckingham RH.
Suppression of thermosensitive peptidyl-tRNA hydrolase mutation in
Escherichia coli by gene duplication.
Microbiology. 2001 Jun;147(Pt 6):1581-9.
PMID: 11390689



Comment:
Oklahoma ID: NGO.379c

Blast Summary:  PSI-Blast Search
NG0379 is orthologously related to AE002433, Neisseria meningitidis, strain MC58, a peptidyl-tRNA hydrolase protein: residues 1-192 are 97% similar to residues 1-192 of NG0379.

Numerous significant hits to peptidyl-tRNA hydrolase proteins in gapped BLAST; e.g. residues 4-191 are 55% similar to gb|AAG56062.1|AE005338_2 peptidyl-tRNA hydrolase of Escherichia coli O157:H7 EDL933, residues 5-191 are 46% similar to gb|AAF85439.1|AE004071_7 peptidyl tRNA hydrolase of Xylella fastidiosa, residues 5-191 are 54% similar to gb|AAB06185.1| peptidyl-tRNA hydrolase of Salmonella typhi.

COGS Summary:  COGS Search
BeTs to 13 clades of COG0193
COG name: Peptidyl-tRNA hydrolase
Functional Class:  J
The phylogenetic pattern of COG0193 is ----yqvcebrhujgpolinx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB001328 (Peptidyl-tRNA hydrolase) with a combined E-value of 5.8e-57.
    IPB001328A    7-26
    IPB001328B    63-74
    IPB001328C    91-122
    IPB001328D    131-141


ProDom Summary:  Protein Domain Search
Residues 5-190 are 51% similar to a (HYDROLASE PEPTIDYL-TRNA PTH PROTEIN) protein domain (PD005324) which is seen in PTH_ECOLI.



Paralogs:  Local Blast Search


NG0379 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 7 to 190 (E-value = 1.5e-95) place NG0379 in the Pept_tRNA_hydro family which is described as Peptidyl-tRNA hydrolase (PF01195)

Structural Feature(s):
Feature Type  Start  Stop
No predicted structural features.  
  

PDB Hit:
pdb|2PTH|2PTH PEPTIDYL-TRNA HYDROLASE FROM ESCHERICHIA COLI 318.0 7e-88

Gene Protein Sequence:
MSNTIKMVVGLGNPGKEYEQTRHNAGFWFLDELAWKWKASFKEEKKFFGE
VARAALPDGDVWLLKPATFMNRSGQAVAALAQFYKIKPEEILVVHDELDI
PCGRIKFKLGGGNGGHNGLKDIQAKLGTADYYRLRLGIGHPGDRNLVVGY
VLNKPSAEHRRQIDDAVAKSLQAVPDIISGKWEEATRFLHSK

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCAAACACAATCAAAATGGTTGTCGGCTTGGGCAACCCGGGCAAAGA
ATACGAACAGACCCGCCACAATGCGGGCTTTTGGTTCCTCGACGAACTGG
CGTGGAAATGGAAGGCTTCGTTTAAAGAAGAAAAAAAATTCTTCGGCGAA
GTTGCCCGCGCCGCCCTGCCCGACGGCGATGTTTGGCTGCTCAAACCGGC
CACGTTCATGAACCGTTCCGGACAGGCGGTTGCCGCGCTTGCACAGTTCT
ACAAAATCAAACCCGAAGAAATCCTCGTCGTCCACGACGAACTCGACATC
CCTTGCGGACGGATCAAATTCAAACTCGGCGGCGGCAACGGCGGACACAA
CGGCTTGAAAGACATTCAGGCAAAACTCGGCACGGCAGACTATTACCGCC
TGCGCCTCGGCATCGGCCACCCCGGCGACCGCAACCTCGTCGTCGGCTAC
GTCTTGAACAAACCGAGCGCGGAACACCGCCGGCAAATCGACGATGCCGT
CGCCAAATCCCTGCAGGCCGTACCCGACATCATTTCCGGCAAATGGGAAG
AGGCAACGCGCTTCCTGCACAGCAAA


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