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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap tRNA-Gly-2 IGR583 IGR582 IGR580 IGR581 IGR584 IGR585 CT702 clpP, - CT706 pcnB, - CT704 clpX, - CT705 tig, - CT707 yphC, - CT703 snf,mot1, - CT708 CT702 clpP, - CT706 pcnB, - CT704 clpX, - CT705 tig, - CT707 yphC, - CT703 snf,mot1, - CT708 CT702 clpP, - CT706 pcnB, - CT704 clpX, - CT705 tig, - CT707 yphC, - CT703 snf,mot1, - CT708
* Calculated from Protein Sequence

Gene ID: CT706

DNA Molecule Name:

Genbank ID:

Gene Name:

ATP-dependent ClpP endopeptidase subunit

Gene Start:

Gene Stop:

Gene Length:

Molecular Weight*:


Net Charge*:


Functional Class:
translation; proteases  

Pathway: pathway table

Secondary Evidence:
Kroh, H.E., L.D. Simon. 1990. "The ClpP component of Clp protease is the sigma
32-dependent heat shock protein F21.5." J.Bacteriol. 172:6026-6034. Maurizi,
M.R., W.P. Clark, Y. Katayama, S. Rudikoff, J. Pumphrey, B. Bowers, S. Gottesman.
1990. "Sequence and structure of ClpP, the proteolytic component of the
ATP-dependent Clp protease of Escherichia coli." J.Biol.Chem. 265:12536-12545.

ClpP ATP-dependent protease Ti proteolytic subunit

In E.coli, this enzyme cleaves peptides internally in a process that requires
ATP. It is a dimeric protein that requires a regulatory subunit (clpA
or clpX) as well as this proteolytic subunit. For the regulatory
subunits, see CT286, CT705, CT113. See CT431 for another clpP sequence.

From Prosite PDOC00358:

The endopeptidase Clp (EC from Escherichia coli cleaves peptides in various proteins in a process that requires ATP hydrolysis. Clp is a dimeric protein which consists of a proteolytic subunit (gene clpP) and either of two related ATP-binding regulatory subunits (genes clpA and clpX). ClpP is a serine protease which has a chymotrypsin-like activity. Its catalytic activity seems to be provided by a charge relay system similar to that of the trypsin family of serine proteases, but which evolved by independent convergent evolution.

Proteases highly similar to ClpP have been found to be encoded in the genome of the chloroplast of plants and seem to be also present in other eukaryotes.

The sequences around two of the residues involved in the catalytic triad (a serine and a histidine) are highly conserved and can be used as signature patterns specific to that category of proteases.

Blast Summary:  PSI-Blast Search
Numerous hits in Psi-BLAST to ATP-dependent endopeptidase subunits, e.g.,
residues 1-193 are 49% similar to CLPP_ECOLI. Residues 176-197 are highly
similar to short stretches of ompB sequences from C.trachomatis, namely
U56926, X53511, U56925.

CT706 is orthologously related to CPn0847: residues 1-200 of CT706 are 95%
similar to residues 1-201 of CPn0847, a predicted ATP-dependent ClpP endopeptidase
subunit from C. pneumoniae.

COGS Summary:  COGS Search
BeTs to 11 clades of COG0740
COG name: Protease subunits of ATP-dependent proteases, ClpP family
Functional Class:  O
The phylogenetic pattern of COG0740 is -----qvCebRhuj--OLINx
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
Residues 19-52, 74-125, 146-189 are significantly matched to blocks
BL00381A,B,C, which encompass endopeptidase CLP sequences, e.g., CLPP_SYNY3,

ProDom Summary:  Protein Domain Search
Residues 19-189 are 56% similar to a CLPP domain as observed in CLPP_HELPY.

Paralogs:  Local Blast Search
CT706 is paralogously related to CT431, also thought to be a CLPP sequence:
residues 23-192 are 39% similar to CT431.

Pfam Summary:  Pfam Search
Residues 12 to 193 (E-value = 1.6e-117) place CT706 in the CLP_protease family which is described as Clp protease (PF00574)

PDB Hit:
gi|3318853|pdb|1TYF|A Chain A, The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For Atp-Dependent Proteolysis Peptidase Mol_id: 1; Molecule: Clp Peptidase; Chain: A, B, C, D, E, F, G, H, I, J, K, L, M, N; Synonym: Clpp; Ec:; Eng

Gene Protein Sequence:

Gene Nucleotide Sequence:  Sequence Viewer

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