uvrB

168

excinuclease ABC (subunit B), required for transcription-dependent asymmetry in mutation rates of genes in the two orientations

Locus: BSU_35170

Molecular weight: 76.15 kDa

Isoelectric point: 5.26

Protein length: 661 aa

Gene length: 1986 bp

Function: DNA repair after UV damage

Product: excinuclease ABC (subunit B)

Essential: no

Synonyms: uvrB, dinA, uvrA

Genomic Context

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List of homologs in different organisms, belongs to COG0556 (Galperin et al., 2021)

Gene

Coordinates: 3,612,945 → 3,614,930

Phenotypes of a mutant

• a uvrA uvrB mutant is sensitive to blue light-induced DNA damage PubMed
• reduced resistance towards electron beams PubMed

The protein

Protein family

• UvrB family (with Mfd, according to UniProt)

Domains

• Helicase ATP-binding domain (aa 26-413) (according to UniProt)
• Helicase C-terminal domain (aa 430-596) (according to UniProt)
• UVR domain (aa 625-660) (according to UniProt)

Structure

• 2NMV (PDB) (bound to fluorescein-adducted DNA); 2D7D (PDB) ternary complex involving UvrB* (a C-terminal truncation of full-length UvrB), a polythymine trinucleotide and ADP PubMed
• P37954 (AlphaFold)

Localization

• cytoplasm (according to Swiss-Prot)

Expression and Regulation

Operons

• Genes: uvrB-uvrA

  Description: PubMed

  Regulation

  • induced upon DNA damage (LexA) PubMed

  Regulatory mechanism

  • LexA: repression, PubMed, in lexA regulon

  Additional information

  • during sporulation expressed both in the forespore and the mother cell PubMed
  • expression is induced in the presence of Cr(VI) PubMed

Biological materials

Mutant

• GP3534 (Δ(uvrA-uvrB)::kan), available in Jörg Stülke's lab
• GP1175 (Δ(uvrA-uvrB)::ermC), available in Jörg Stülke's lab PubMed
• BKE35170 (ΔuvrB::erm  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CACAAAAATAAGCCTCCGTT,  downstream forward: _UP4_CTAAAAGCGGAAGGATGATG
• BKK35170 (ΔuvrB::kan  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CACAAAAATAAGCCTCCGTT,  downstream forward: _UP4_CTAAAAGCGGAAGGATGATG

References

Reviews

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Original Publications

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