Difference between revisions of "UvrB"

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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
** [[UvrA]]-[[UvrB]] {{PubMed|16464004}}
+
** [[UvrA]]-[[UvrB]] {{PubMed|16464004}}
 
** [[UvrB]]-[[UvrC]] {{PubMed|16464004}}
 
** [[UvrB]]-[[UvrC]] {{PubMed|16464004}}
 
** [[UvrB]] interacts sequentially with [[UvrA]] and [[UvrC]], a complex of the three proteins was never observed {{PubMed|16464004}}
 
** [[UvrB]] interacts sequentially with [[UvrA]] and [[UvrC]], a complex of the three proteins was never observed {{PubMed|16464004}}
 +
** [[UvrB]]-[[PcrA]] {{PubMed|24147116}}
  
 
* '''[[Localization]]:''' cytoplasm (according to Swiss-Prot)
 
* '''[[Localization]]:''' cytoplasm (according to Swiss-Prot)
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<pubmed>16464004 15927210 7801120  22933559 </pubmed>
 
<pubmed>16464004 15927210 7801120  22933559 </pubmed>
 
== Original publications ==
 
== Original publications ==
<pubmed>8226626, 9555905 16426634 21821766</pubmed>
+
<pubmed>8226626, 9555905 16426634 21821766 24147116</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 18:46, 17 November 2013

  • Description: excinuclease ABC (subunit B)

Gene name uvrB
Synonyms dinA, uvrA
Essential no
Product excinuclease ABC (subunit B)
Function DNA repair after UV damage
Gene expression levels in SubtiExpress: uvrB
Interactions involving this protein in SubtInteract: UvrB
MW, pI 76 kDa, 5.26
Gene length, protein length 1983 bp, 661 aa
Immediate neighbours uvrA, csbA
Sequences Protein DNA DNA_with_flanks
Genetic context
UvrB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
UvrB expression.png















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

  • A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed


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:

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

Original publications

Emma J Gwynn, Abigail J Smith, Colin P Guy, Nigel J Savery, Peter McGlynn, Mark S Dillingham
The conserved C-terminus of the PcrA/UvrD helicase interacts directly with RNA polymerase.
PLoS One: 2013, 8(10);e78141
[PubMed:24147116] [WorldCat.org] [DOI] (I e)

Christopher T Brown, Laura K Fishwick, Binna M Chokshi, Marissa A Cuff, Jay M Jackson, Travis Oglesby, Alison T Rioux, Enrique Rodriguez, Gregory S Stupp, Austin H Trupp, James S Woollcombe-Clarke, Tracy N Wright, William J Zaragoza, Jennifer C Drew, Eric W Triplett, Wayne L Nicholson
Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.
Appl Environ Microbiol: 2011, 77(19);6867-77
[PubMed:21821766] [WorldCat.org] [DOI] (I p)

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)