Basic Search | Intermediate Search | Advanced SQL Search | Gene Image Map |  Home

Chlamydia pneumoniae Search Results

Record: 1 of 1  
MiniMap tRNA_Gly_2 IGR676 IGR675 IGR671 IGR673 IGR672 IGR674 IGR677 IGR678 CPn0842 CPn0843 clpP_2, - CPn0847 pcnB_1, - CPn0845 clpX, - CPn0846 tig, - CPn0848 yphC, - CPn0844 snf,mot1, - CPn0849 CPn0842 CPn0843 clpP_2, - CPn0847 pcnB_1, - CPn0845 clpX, - CPn0846 tig, - CPn0848 yphC, - CPn0844 snf,mot1, - CPn0849 CPn0843 clpP_2, - CPn0847 pcnB_1, - CPn0845 clpX, - CPn0846 tig, - CPn0848 yphC, - CPn0844 CPn0842 snf,mot1, - CPn0849
* Calculated from Protein Sequence

Gene ID: CPn0847

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
clpP_2  

Definition:
ATP-dependent ClpP endopeptidase subunit

Gene Start:
959995

Gene Stop:
959384

Gene Length:
612

Molecular Weight*:
22066

pI*:
5.10

Net Charge*:
-5.18

EC:
3.4.21.92  

Functional Class:
protein fate; degradation of proteins, peptides and glycoproteins  

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.

Comment:
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 CPn0437, CPn0144, CPn0846. See CPn0520 for another clpP sequence.

From Prosite PDOC00358:

The endopeptidase Clp (EC 3.4.21.92) 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
CPn0847 is orthologously related to CT706: residues 1-201 of CPn0847 are 95% similar to residues 1-200 of CT706, a predicted ATP-dependent ClpP endopeptidase subunit from C. trachomatis.
CPn0847 is also similar to TP0507, CT431, TP1041, all ATP-dependent Clp proteases.

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 1

Blocks Summary:  Blocks Search


ProDom Summary:  Protein Domain Search


Paralogs:  Local Blast Search
CPn0847 is paralogous to CPn0520: residues 20-192 of CPn0847 are 41% similar to residues 13-187 of CPN0520, a predicted Clp protease from C. pneumoniae.

Pfam Summary:  Pfam Search
Residues 12 to 193 (E-value = 9.5e-119) place CPn0847 in the CLP_protease family which is described as Clp protease (PF00574)

PDB Hit:


Gene Protein Sequence:
MTLVPYVVEDTGRGERAMDIYSRLLKDRIVMIGQEITEPLANTVIAQLLF
LMSEDPKKDIQIFINSPGGYITAGLAIYDTIRFLGCDVNTYCIGQAASMG
ALLLSAGTKGKRHALPHSRMMIHQPSGGIIGTSADIQLQAAEILTLKKHL
ANILSECTGQPVEKIIEDSERDFFMGAEEAISYGLIDKVVTSAKETNKDT
SST$

Gene Nucleotide Sequence:  Sequence Viewer
ATGACACTGGTACCCTATGTTGTCGAGGATACGGGCCGTGGTGAAAGGGC
CATGGATATTTACTCCCGTCTTCTGAAAGATCGTATTGTAATGATCGGTC
AGGAAATCACGGAGCCCCTCGCAAACACAGTAATTGCCCAGCTCCTTTTC
CTCATGTCCGAAGATCCTAAAAAGGATATTCAAATTTTCATCAATTCCCC
AGGCGGCTACATCACCGCTGGACTGGCAATCTATGATACCATTCGCTTTT
TAGGTTGTGATGTAAATACCTACTGCATCGGTCAAGCTGCATCCATGGGA
GCCCTCTTATTATCCGCAGGAACTAAAGGAAAGCGTCACGCTCTTCCCCA
TAGCCGTATGATGATCCACCAACCTTCTGGAGGCATTATCGGAACATCCG
CAGACATCCAACTCCAAGCAGCTGAAATTCTAACACTAAAAAAACACCTT
GCCAATATCCTCTCTGAATGCACAGGACAACCTGTAGAAAAAATTATAGA
AGATTCTGAACGAGATTTCTTCATGGGAGCCGAGGAAGCCATCTCCTACG
GACTTATTGATAAGGTGGTAACTTCTGCGAAAGAAACTAATAAGGATACA
AGTAGCACTTAG


Los Alamos National Laboratory     
Operated by the University of California for the National Nuclear Security Administration,
of the US Department of Energy.     Copyright © 2001 UC | Disclaimer/Privacy