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Chlamydia pneumoniae Search Results

Record: 1 of 1  
MiniMap tRNA_Asn_1 IGR109 IGR107 IGR111 IGR113 IGR112 IGR110 IGR108 IGR114 groES, - CPn0135 CPn0130 CPn0129 ybgI, - CPn0137 CPn0133 hemL, - CPn0138 groEL, - CPn0134 pepF, - CPn0136 CPn0132 CPn0131 groES, - CPn0135 CPn0130 CPn0129 ybgI, - CPn0137 CPn0133 hemL, - CPn0138 groEL, - CPn0134 pepF, - CPn0136 CPn0132 CPn0131 groES, - CPn0135 CPn0129 ybgI, - CPn0137 CPn0133 hemL, - CPn0138 groEL, - CPn0134 pepF, - CPn0136 CPn0130 CPn0132 CPn0131
* Calculated from Protein Sequence

Gene ID: CPn0134

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
groEL  

Definition:
60 kD chaperonin (heatshock protein GroEL)

Gene Start:
169098

Gene Stop:
167464

Gene Length:
1635

Molecular Weight*:
58194

pI*:
5.20

Net Charge*:
-11.72

EC:
 

Functional Class:
cellular processes; chaperones  

Pathway: pathway table

Primary Evidence:
Cerrone MC, Ma JJ, Stephens RS. 1991. Cloning and sequence of the gene for heat shock protein 60 from Chlamydia trachomatis and immunological reactivity of the protein. Infect. Immun. 59(1):79-90.

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, 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:
Promotes proper folding of unfolded proteins under stress conditions. GroEL has
been implicated in chlamydial pathogenesis (inflammation and scarring). See CPn0135 for C. pneumoniae GroES.
For GroEL, see CPn0777 and CPn0898.

From Prosite PDOC00268:

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 cpn60 protein shows weak ATPase activity and is a highly conserved protein
of about 550 to 580 amino acid residues which has been described by different
names in different species.



Blast Summary:  PSI-Blast Search
CPn0134 is orthologously related to CT110: residues 1-544 of CPn0134 are 91% similar to residues 1-544 of CT110, a predicted 60 kD chaperonin (protein cpn60, GroEL protein) & (57 kD chlamydial hypersensitivity antigen; HSP60) from C. trachomatis.
CPn0134 is also similar to TP0030, MG392, CT604, CT755, all predicted heat shock proteins.

COGS Summary:  COGS Search
BeTs to 17 clades of COG0459
COG name: Chaperonin GroEL (HSP60 family)
Functional Class:  O
The phylogenetic pattern of COG0459 is AmTkYqvCebRhujgpolINx
Number of proteins in this genome belonging to this COG is 3

Blocks Summary:  Blocks Search


ProDom Summary:  Protein Domain Search


Paralogs:  Local Blast Search
CPn0134 is paralogous to CPn0777 and CPn0898, both predicted HSP-60: residues 11-524 of CPn0134 are 35% similar to residues 10-521 of CPn0777; residues 9-532 of CPn0134 are 26% similar to residues 9-518 of CPn0898.

Pfam Summary:  Pfam Search
Residues 23 to 527 (E-value = 2.4e-184) place CPn0134 in the Cpn60_TCP1 family which is described as TCP-1/cpn60 chaperonin family (PF00118)

Structural Feature(s):
Feature Type  Start  Stop
coil-coil  
346  
375
non-globular  
472  
544

PDB Hit:


Gene Protein Sequence:
MAAKNIKYNEEARKKIHKGVKTLAEAVKVTLGPKGRHVVIDKSFGSPQVT
KDGVTVAKEIELEDKHENMGAQMVKEVASKTADKAGDGTTTATVLAEAIY
SEGLRNVTAGANPMDLKRGIDKAVKVVVDELKKISKPVQHHKEIAQVATI
SANNDSEIGNLIAEAMEKVGKNGSITVEEAKGFETVLDVVEGMNFNRGYL
SSYFSTNPETQECVLEDALILIYDKKISGIKDFLPVLQQVAESGRPLLII
AEEIEGEALATLVVNRLRAGFRVCAVKAPGFGDRRKAMLEDIAILTGGQL
VSEELGMKLENTTLAMLGKAKKVIVTKEDTTIVEGLGNKPDIQARCDNIK
KQIEDSTSDYDKEKLQERLAKLSGGVAVIRVGAATEIEMKEKKDRVDDAQ
HATIAAVEEGILPGGGTALVRCIPTLEAFLPMLANEDEAIGTRIILKALT
APLKQIASNAGKEGAIICQQVLARSANEGYDALRDAYTDMIDAGILDPTK
VTRSALESAASIAGLLLTTEALIADIPEEKSSSAPAMPSAGMDY$

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCAGCGAAAAATATTAAATATAATGAAGAAGCCAGAAAAAAAATACA
TAAAGGGGTAAAAACTCTTGCAGAAGCAGTAAAAGTTACTCTAGGTCCTA
AAGGACGTCACGTAGTTATAGATAAGAGCTTTGGCTCTCCCCAAGTGACT
AAAGATGGTGTTACTGTAGCTAAAGAAATCGAGCTCGAAGACAAACATGA
AAACATGGGCGCTCAGATGGTAAAAGAAGTCGCCAGCAAAACTGCTGACA
AAGCAGGCGACGGAACTACAACAGCAACTGTTCTTGCAGAAGCAATCTAT
AGCGAAGGTCTAAGAAATGTCACTGCCGGTGCCAATCCTATGGACCTAAA
AAGAGGTATCGACAAAGCCGTAAAAGTTGTTGTTGATGAACTCAAAAAAA
TTAGTAAACCTGTACAACATCACAAAGAAATCGCTCAAGTAGCTACTATC
TCAGCAAATAATGATTCCGAAATCGGAAATCTTATTGCAGAAGCTATGGA
AAAAGTTGGTAAAAACGGATCCATTACTGTTGAAGAAGCTAAAGGCTTCG
AAACTGTTCTCGACGTTGTAGAAGGAATGAACTTCAACCGTGGATACCTC
TCCAGCTACTTCTCCACAAATCCAGAAACTCAAGAATGCGTTTTAGAAGA
CGCTCTGATTCTAATCTACGATAAAAAAATCTCTGGAATTAAAGACTTCC
TTCCAGTTTTACAACAAGTAGCAGAATCTGGACGCCCTCTTTTAATCATT
GCAGAAGAAATTGAAGGAGAAGCTTTAGCAACTCTAGTAGTCAATAGACT
CCGTGCAGGATTCAGAGTCTGTGCAGTGAAAGCTCCTGGTTTCGGTGACA
GAAGAAAAGCTATGTTAGAAGACATCGCTATCCTTACTGGTGGCCAACTA
GTTAGCGAAGAACTTGGCATGAAACTAGAGAATACAACTCTAGCAATGTT
AGGAAAAGCTAAGAAAGTTATCGTAACTAAAGAAGATACCACAATCGTCG
AAGGCTTAGGAAACAAACCTGATATCCAAGCTCGATGCGACAATATTAAA
AAACAAATCGAAGATAGCACTTCAGATTACGACAAAGAAAAACTCCAAGA
GCGTTTAGCTAAACTCTCCGGTGGTGTCGCCGTAATCCGCGTAGGAGCTG
CTACCGAAATAGAGATGAAAGAGAAAAAAGACAGAGTAGATGATGCACAA
CACGCAACCATTGCAGCTGTCGAAGAAGGAATCCTCCCTGGTGGTGGAAC
TGCCTTAGTTCGCTGTATCCCTACACTAGAAGCTTTCCTTCCTATGCTAG
CAAACGAAGACGAAGCTATTGGTACTCGTATTATTCTAAAAGCATTAACA
GCTCCATTAAAGCAAATTGCAAGTAACGCAGGTAAAGAAGGCGCTATCAT
TTGTCAGCAAGTTCTAGCAAGATCTGCAAATGAAGGCTATGATGCTTTAC
GTGACGCTTATACAGATATGATTGACGCAGGAATTTTAGATCCAACTAAA
GTGACTCGCTCAGCTCTAGAAAGCGCAGCTTCTATCGCAGGATTACTCCT
CACAACAGAAGCCTTAATCGCTGATATCCCAGAAGAGAAATCTTCTTCAG
CTCCAGCGATGCCAAGCGCAGGAATGGACTACTAG


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