| General information | | DisProt: | DP00626 | | Name: | Protein umuD | | Synonym(s): | UMUD_ECOLI
Protein umuD' [cleavage product 1]
| | First appeared in release: | Release 5.2 (08/07/2010) | | UniProt: | P0AG11 | | UniGene: | | | SwissProt: | UMUD_ECOLI | | TrEMBL: | | | NCBI (GI): | 84029418 | | Source organism: | Escherichia coli (strain K12) | | Sequence length: | 139 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MLFIKPADLR EIVTFPLFSD LVQCGFPSPA ADYVEQRIDL NQLLIQHPSA TYFVKASGDS - 60
MIDGGISDGD LLIVDSAITA SHGDIVIAAV DGEFTVKKLQ LRPTVQLIPM NSAYSPITIS - 120
SEDTLDVFGV VIHVVKAMR
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| Functional narrative |
Involved in UV protection and mutation. Essential for induced (or SOS) mutagenesis. May modify the DNA replication machinery to allow bypass synthesis across a damaged template.
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| 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.
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| Region 1 | | Type: | Disordered | | Name: | Whole protein | | Location: | 1 - 139 | | Length: | 139 | | Region sequence: |
MLFIKPADLREIVTFPLFSDLVQCGFPSPAADYVEQRIDLNQLLIQHPSATYFVKASGDS
MIDGGISDGDLLIVDSAITASHGDIVIAAVDGEFTVKKLQLRPTVQLIPMNSAYSPITIS
SEDTLDVFGVVIHVVKAMR | | Modification type: | Native
| | PDB: | 1AY9:A, 1I4V:A, 1UMU:A | | Structural/functional type: | Function arises via a molten globule to order transition
| | Functional classes: | Modification site
Molecular recognition effectors
Entropic chain
| | Functional subclasses: | Protein-DNA binding
Protein-protein binding
Entropic clock
| Detection methods:
- Sensitivity to proteolysis (310 K; Chymotrypsin (1:1) 5 mg/mL; UmuD(2) dimer 10 uM)
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 6.8; DTT (buffer) 1 mM; EDTA (buffer) 0.1 mM; Interacting protein (DinB or beta-subunit) 50 uM; Na3PO4 (buffer (pH 6.8)) 10 mM; NaCl (buffer) 100 mM; UmuD (at physio concentrations or w/interacting protein at >/= 50uM))
- Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 7.4; Glycerol (buffer (5%)); Hepes (buffer (7.4 pH)) 50 mM; Interacting protein (DinB or beta-subunit) 50 uM; KCl (buffer) 100 mM; MgCl2 (buffer) 5 mM; UmuD (at physio concentrations or w/interacting protein at >/= 50uM))
| References:
- Simon SM, Sousa FJ, Mohana-Borges R, Walker GC. "Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products." Proc Natl Acad Sci U S A. 2008; 105(4): 1152-7. PubMed: 18216271
| Comments:
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| References |
- Ferentz AE, Walker GC, Wagner G. "Converting a DNA damage checkpoint effector (UmuD2C) into a lesion bypass polymerase (UmuD'2C)." EMBO J.. 2001; 20(15): 4287-98. PubMed: 11483531
- Peat TS, Frank EG, McDonald JP, Levine AS, Woodgate R, Hendrickson WA. "The UmuD' protein filament and its potential role in damage induced mutagenesis." Structure. 1996; 4(12): 1401-12. PubMed: 8994967
- Peat TS, Frank EG, McDonald JP, Levine AS, Woodgate R, Hendrickson WA. "Structure of the UmuD' protein and its regulation in response to DNA damage." Nature. 1996; 380(6576): 727-30. PubMed: 8614470
- Simon SM, Sousa FJ, Mohana-Borges R, Walker GC. "Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products." Proc Natl Acad Sci U S A. 2008; 105(4): 1152-7. PubMed: 18216271
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| Comments |
UmuD operates in homodimeric form.
AV (7-7-2010) PubMed: 18216271
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