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Chlamydia pneumoniae Search Results

Record: 1 of 1  
MiniMap tRNA_Asn_1 IGR109 IGR111 IGR115 IGR113 IGR112 IGR110 IGR108 IGR114 groES, - CPn0135 yqgE, - CPn0139 ybgI, - CPn0137 CPn0133 hemL, - CPn0138 groEL, - CPn0134 pepF, - CPn0136 CPn0132 CPn0131 groES, - CPn0135 yqgE, - CPn0139 ybgI, - CPn0137 CPn0133 hemL, - CPn0138 groEL, - CPn0134 pepF, - CPn0136 CPn0132 CPn0131 groES, - CPn0135 yqgE, - CPn0139 ybgI, - CPn0137 CPn0133 hemL, - CPn0138 groEL, - CPn0134 pepF, - CPn0136 CPn0132 CPn0131
* Calculated from Protein Sequence

Gene ID: CPn0135

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
groES  

Definition:
10 kD chaperonin, GroES

Gene Start:
169448

Gene Stop:
169140

Gene Length:
309

Molecular Weight*:
11299

pI*:
4.50

Net Charge*:
-6.00

EC:
 

Functional Class:
cellular processes; chaperones  

Pathway: pathway table

Primary Evidence:
Ho Y and Zhang YX. 1994. The sequence of the groES and groEL genes
from the mouse pneumonitis agent of Chlamydia-trachomatis. Gene
141(1): 143-144. Mayr M, Metzler B, Kiechl S, Willeit J, Schett G,

Mayr M, Metzler B,
Kiechl S, Willeit J, Schett G, Xu QB, Wick G. 1999. Endothelial cytotoxicity mediated by
serum antibodies to heat shock proteins of Escherichia coli and Chlamydia pneumoniae: Immune
reactions to heat shock proteins as a possible link between infection and atherosclerosis.
Circulation 99(12): 1560-1566.

Comment:
Chaperonins form oligomeric complexes composed of two different types of
subunits: a 60 Kd protein, known as cpn60 (or groEL) that is highly conserved
and a 10 Kd protein, known as cpn10 (or groES). CPn0134, CPn0604, CPn0755 are cpn60
sequences.

From Prosite PDOC00576:

Chaperonins are proteins involved in the folding of proteins or the assembly of
oligomeric protein complexes. Their role seems to be to assist other
polypeptides to maintain or assume conformations which permit their correct
assembly into oligomeric structures. They are found in abundance in prokaryotes,
chloroplasts and mitochondria. Chaperonins form oligomeric complexes and are
composed of two different types of subunits: a 60 kD protein, known as cpn60
(groEL in bacteria) and a 10 kD protein, known as cpn10 (groES in bacteria).

The cpn10 protein binds to cpn60 in the presence of MgATP and suppresses the
ATPase activity of the latter. Cpn10 is a protein of about 100 amino acid
residues whose sequence is well conserved in bacteria, vertebrate mitochondria
and plants chloroplast. Cpn10 assembles as an heptamer that forms a dome.

Blast Summary:  PSI-Blast Search
CPn0135 is orthologously related to CT111: residues 1-102 of CPn0135 are 78% similar to residues 1-102 of CT111, a predicted 10kD chaperonin from C. trachomatis.
CPn0135 is slightly similar to TP1013, heat shock protein GroES from T. pallidum.

COGS Summary:  COGS Search
BeTs to 13 clades of COG0234
COG name: Co-chaperonin GroES (HSP10)
Functional Class:  O
The phylogenetic pattern of COG0234 is ----yqvcebrhujgpolinx
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
No paralogs in C. pneumoniae.

Pfam Summary:  Pfam Search
Residues 9 to 102 (E-value = 3.4e-54) place CPn0135 in the Cpn10 family which is described as Chaperonin 10 Kd subunit (PF00166)

PDB Hit:


Gene Protein Sequence:
MSDQATTLRIKPLGDRILVKREEEEATARGGIILPDTAKKKQDRAEVLVL
GTGKRTDDGTLLPFEVQVGDIILMDKYAGQEITIDDEEYVILQSSEIMAV
LK$

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCTGATCAAGCAACGACCCTCCGAATTAAACCTTTGGGCGATAGAAT
CTTGGTAAAAAGGGAAGAAGAAGAAGCCACTGCTCGTGGAGGAATCATCT
TACCCGATACAGCAAAAAAGAAACAAGATCGTGCTGAGGTCCTTGTTTTA
GGCACAGGCAAACGAACTGATGACGGTACTCTACTTCCTTTCGAAGTTCA
AGTTGGCGATATCATTTTAATGGATAAGTATGCAGGTCAAGAAATCACAA
TCGATGACGAAGAGTATGTCATTCTACAGTCCAGTGAAATCATGGCCGTC
CTAAAATAA


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