DP00412: 10 kDa chaperoninFASTA viewXML view

General information
DisProt:DP00412
Name:10 kDa chaperonin
Synonym(s):CH10_ECO57
Protein Cpn10
groES protein
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P0A6G1
UniGene: 
SwissProt: CH10_ECO57
TrEMBL:  
NCBI (GI): 62288020
Source organism:Escherichia coli O157:H7
Sequence length:97
Percent disordered:15%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE NGEVKPLDVK - 60
VGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA



Functional narrative    

Type I chaperonins play an essential role in the folding of newly translated and stress-denatured proteins in eubacteria, mitochondria and chloroplasts. GroES consists of seven identical 10 kDa subunits and is involved in assisting protein folding as the partner of another oligomeric protein, the GroEL chaperonin. Each GroES subunit uses a mobile loop with a conserved hydrophobic tripeptide for interaction with GroEL. The mobile loops are ∼16 amino acids in length and undergo a transition from disordered loops to beta-hairpins concomitant with binding the apical domains of GroEL. Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.

Region 1: 17-31

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name:Mobile loop
Location:17 - 31
Length:15
Region sequence:

VETKSAGGIVLTGSA

Modification type: Native
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Chaperones
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (303 K; pH: 6.5; Potassium phosphate 45 mM)

References:
  1. Csizmók V, Szollosi E, Friedrich P, Tompa P. "A novel two-dimensional electrophoresis technique for the identification of intrinsically unstructured proteins." Mol Cell Proteomics. 2006; 5(2): 265-73. PubMed: 16223749

  2. Landry SJ, Taher A, Georgopoulos C, van der Vies SM. "Interplay of structure and disorder in cochaperonin mobile loops." Proc Natl Acad Sci U S A. 1996; 93(21): 11622-7. PubMed: 8876186

  3. Shewmaker F, Kerner MJ, Hayer-Hartl M, Klein G, Georgopoulos C, Landry SJ. "A mobile loop order-disorder transition modulates the speed of chaperonin cycling." Protein Sci. 2004; 13(8): 2139-48. PubMed: 15238634

Comments:
 



References

  1. Shewmaker F, Kerner MJ, Hayer-Hartl M, Klein G, Georgopoulos C, Landry SJ. "A mobile loop order-disorder transition modulates the speed of chaperonin cycling." Protein Sci. 2004; 13(8): 2139-48. PubMed: 15238634

  2. Walter S. "Structure and function of the GroE chaperone." Cell Mol Life Sci. 2002; 59(10): 1589-97. PubMed: 12475168



Comments


Additional UniProt ID: P0A6F9 strain K12 (B178) was also used.


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