Difference between revisions of "UvrB"

From SubtiWiki
Jump to: navigation, search
(Biological materials)
Line 109: Line 109:
 
=Biological materials =
 
=Biological materials =
  
* '''Mutant:''' GP1175 (''uvrAB''::''ermC'') (available in the [[Stülke]] lab)  
+
* '''Mutant:''' GP1175 (''del uvrAB''::''ermC'') (available in the [[Stülke]] lab)  
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''

Revision as of 16:11, 7 February 2011

  • Description: excinuclease ABC (subunit B)

Gene name uvrB
Synonyms dinA, uvrA
Essential no
Product excinuclease ABC (subunit B)
Function DNA repair after UV damage
MW, pI 76 kDa, 5.26
Gene length, protein length 1983 bp, 661 aa
Immediate neighbours uvrA, csbA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
UvrB context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

DNA repair/ recombination

This gene is a member of the following regulons

LexA regulon

The gene

Basic information

  • Locus tag: BSU35170

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: uvrB family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure: 2NMV (bound to fluorescein-adducted DNA); 2D7D ternary complex involving UvrB* (a C-terminal truncation of full-length UvrB), a polythymine trinucleotide and ADP PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP1175 (del uvrAB::ermC) (available in the Stülke lab)
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

James J Truglio, Deborah L Croteau, Bennett Van Houten, Caroline Kisker
Prokaryotic nucleotide excision repair: the UvrABC system.
Chem Rev: 2006, 106(2);233-52
[PubMed:16464004] [WorldCat.org] [DOI] (P p)

Bennett Van Houten, Deborah L Croteau, Matthew J DellaVecchia, Hong Wang, Caroline Kisker
'Close-fitting sleeves': DNA damage recognition by the UvrABC nuclease system.
Mutat Res: 2005, 577(1-2);92-117
[PubMed:15927210] [WorldCat.org] [DOI] (P p)

A Sancar
Mechanisms of DNA excision repair.
Science: 1994, 266(5193);1954-6
[PubMed:7801120] [WorldCat.org] [DOI] (P p)

Original Publications

Jitka Eryilmaz, Simona Ceschini, James Ryan, Stella Geddes, Timothy R Waters, Tracey E Barrett
Structural insights into the cryptic DNA-dependent ATPase activity of UvrB.
J Mol Biol: 2006, 357(1);62-72
[PubMed:16426634] [WorldCat.org] [DOI] (P p)

K W Winterling, D Chafin, J J Hayes, J Sun, A S Levine, R E Yasbin, R Woodgate
The Bacillus subtilis DinR binding site: redefinition of the consensus sequence.
J Bacteriol: 1998, 180(8);2201-11
[PubMed:9555905] [WorldCat.org] [DOI] (P p)

C M Lovett, K C Cho, T M O'Gara
Purification of an SOS repressor from Bacillus subtilis.
J Bacteriol: 1993, 175(21);6842-9
[PubMed:8226626] [WorldCat.org] [DOI] (P p)