Ung

• Description: uracil-DNA glycosylase
  
  

Gene name	ung
Synonyms	ipa-57d, ywdG
Essential	no
Product	uracil-DNA glycosylase
Function	DNA repair
Gene expression levels in SubtiExpress: ung
Interactions involving this protein in SubtInteract: Ung
MW, pI	25 kDa, 8.782
Gene length, protein length	675 bp, 225 aa
Immediate neighbours	ywdH, ywdF
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

DNA repair/ recombination

The gene

Basic information

• Locus tag: BSU37970

Phenotypes of a mutant

• increased mutation rates PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: removes uracil preferentially from single-stranded DNA over double-stranded DNA, exhibiting higher preference for U:G than U:A mismatches PubMed

• Protein family: uracil-DNA glycosylase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • SsbA-Ung PubMed

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 3A7N (from Mycobacterium tuberculosis, 42% identity) PubMed

• UniProt: P39615

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: ung PubMed

• Expression browser: ung PubMed

• Sigma factor:

• Regulation:
  • expressed throughout growth and staionary phase PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Original publications

Karina López-Olmos, Martha P Hernández, Jorge A Contreras-Garduño, Eduardo A Robleto, Peter Setlow, Ronald E Yasbin, Mario Pedraza-Reyes
Roles of endonuclease V, uracil-DNA glycosylase, and mismatch repair in Bacillus subtilis DNA base-deamination-induced mutagenesis.
J Bacteriol: 2012, 194(2);243-52
[PubMed:22056936] [WorldCat.org] [DOI] (I p)

Laura Pérez-Lago, Gemma Serrano-Heras, Benito Baños, José M Lázaro, Martín Alcorlo, Laurentino Villar, Margarita Salas
Characterization of Bacillus subtilis uracil-DNA glycosylase and its inhibition by phage φ29 protein p56.
Mol Microbiol: 2011, 80(6);1657-66
[PubMed:21542855] [WorldCat.org] [DOI] (I p)

Audrey Costes, François Lecointe, Stephen McGovern, Sophie Quevillon-Cheruel, Patrice Polard
The C-terminal domain of the bacterial SSB protein acts as a DNA maintenance hub at active chromosome replication forks.
PLoS Genet: 2010, 6(12);e1001238
[PubMed:21170359] [WorldCat.org] [DOI] (I e)

Prem Singh Kaushal, Ramappa K Talawar, Umesh Varshney, M Vijayan
Structure of uracil-DNA glycosylase from Mycobacterium tuberculosis: insights into interactions with ligands.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2010, 66(Pt 8);887-92
[PubMed:20693660] [WorldCat.org] [DOI] (I p)

E Presecan, I Moszer, L Boursier, H Cruz Ramos, V de la Fuente, M-F Hullo, C Lelong, S Schleich, A Sekowska, B H Song, G Villani, F Kunst, A Danchin, P Glaser
The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees).
Microbiology (Reading): 1997, 143 ( Pt 10);3313-3328
[PubMed:9353933] [WorldCat.org] [DOI] (P p)