Difference between revisions of "UvrB"
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU35170&redirect=T BSU35170] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/uvrBA.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/uvrBA.html] | ||
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU35170&redirect=T BSU35170] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2NMV 2NMV] (bound to fluorescein-adducted DNA); [http://www.rcsb.org/pdb/explore.do?structureId=2D7D 2D7D] ternary complex involving UvrB* (a C-terminal truncation of full-length UvrB), a polythymine trinucleotide and ADP {{PubMed|16426634}} | * '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2NMV 2NMV] (bound to fluorescein-adducted DNA); [http://www.rcsb.org/pdb/explore.do?structureId=2D7D 2D7D] ternary complex involving UvrB* (a C-terminal truncation of full-length UvrB), a polythymine trinucleotide and ADP {{PubMed|16426634}} | ||
Revision as of 14:54, 2 April 2014
- 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 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU35170
Phenotypes of a mutant
Database entries
- BsubCyc: BSU35170
- 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:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- BsubCyc: BSU35170
- 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
- UniProt: P37954
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- 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
Justin S Lenhart, Jeremy W Schroeder, Brian W Walsh, Lyle A Simmons
DNA repair and genome maintenance in Bacillus subtilis.
Microbiol Mol Biol Rev: 2012, 76(3);530-64
[PubMed:22933559]
[WorldCat.org]
[DOI]
(I p)
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
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)
Laura Manelyte, Young-In T Kim, Abigail J Smith, Rachel M Smith, Nigel J Savery
Regulation and rate enhancement during transcription-coupled DNA repair.
Mol Cell: 2010, 40(5);714-24
[PubMed:21145481]
[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)
