DP00293: Prokaryotic ubiquitin-like protein pupFASTA viewXML view

General information
DisProt:DP00293
Name:Prokaryotic ubiquitin-like protein pup
Synonym(s):PUP_MYCTU
Bacterial ubiquitin-like modifier
First appeared in release:Release 5.5 (11/17/2010)
UniProt:O33246
UniGene: 
SwissProt: PUP_MYCTU
TrEMBL:  
NCBI (GI): 81669083
Source organism:Mycobacterium tuberculosis
Sequence length:64
Percent disordered:77%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MAQEQTKRGG GGGDDDDIAG STAAGQERRE KLTEETDDLL DEIDDVLEEN AEDFVRAYVQ - 60
KGGQ



Functional narrative    

Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation. Identified substrates are the fabD, panB and mpa proteins.

Region 1: 1-31 Region 2: 33-38 Region 3: 41-45 Region 4: 50-51 Region 5: 60-64

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: 
Location:1 - 31
Length:31
Region sequence:

MAQEQTKRGGGGGDDDDIAGSTAAGQERREK

Modification type: Native
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes:  
Functional subclasses:  
Detection methods:
  1. Nuclear magnetic resonance (NMR) (293 K; pH: 6.8; )

References:
  1. Chen X, Solomon WC, Kang Y, Cerda-Maira F, Darwin KH, Walters KJ. "Prokaryotic ubiquitin-like protein pup is intrinsically disordered." J Mol Biol. 2009; 392(1): 208-17. PubMed: 19607839

  2. Liao S, Shang Q, Zhang X, Zhang J, Xu C, Tu X. Biochem J. 2009 Jul 7. "PUP, a prokaryotic ubiquitin-like protein, is an an intrinsically disordered protein." Biochem J. 2009. PubMed: 18832610

Comments:
 



Region 2
Type:Disordered
Name: 
Location:33 - 38
Length:6
Region sequence:

TEETDD

Modification type: Native
PDB:  
Structural/functional type: Function arises via an order to disorder transition
Functional classes:  
Functional subclasses: Protein-protein binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 6.5; )

References:
There are no documents referencing this region.
Comments:
 



Region 3
Type:Disordered
Name: 
Location:41 - 45
Length:5
Region sequence:

DEIDD

Modification type: Complex
PDB:  
Structural/functional type: Function arises from the disordered state
Functional classes: Modification site
Molecular recognition effectors
Functional subclasses: Protein-protein binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV

  2. Nuclear magnetic resonance (NMR)

References:
There are no documents referencing this region.
Comments:
 



Region 4
Type:Disordered
Name: 
Location:50 - 51
Length:2
Region sequence:

NA

Modification type: Native
PDB:  
Structural/functional type: Function arises via an order to disorder transition
Functional classes:  
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (293 K; pH: 6.8; )

References:
There are no documents referencing this region.
Comments:
 



Region 5
Type:Disordered - Extended
Name: 
Location:60 - 64
Length:5
Region sequence:

QKGGQ

Modification type: Native
PDB:  
Structural/functional type: Function arises via an order to disorder transition
Functional classes:  
Functional subclasses: Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (293 K; pH: 6.8; )

References:
There are no documents referencing this region.
Comments:
 



References

  1. Liao S, Shang Q, Zhang X, Zhang J, Xu C, Tu X. Biochem J. 2009 Jul 7. "PUP, a prokaryotic ubiquitin-like protein, is an an intrinsically disordered protein." Biochem J. 2009. PubMed: 18832610



Comments


Author Verified 11-5-2010 PubMed: 18832610


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