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thrR [2019-02-06 09:44:45]
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thrR [2019-02-06 09:44:45]

transcription repressor of threonine biosynthetic genes
Locus
BSU27910
Isoelectric point
6.36
Molecular weight
16.52 kDa
Protein length
147 aa Sequence Blast
Gene length
444 bp Sequence Blast
Function
control of threonine biosynthesis
Product
transcription repressor of threonine biosynthetic genes
Essential
no
Synonyms
pheB,yszB

Genomic Context

      
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Categories containing this gene/protein

Gene

Coordinates
2,852,157 2,852,600

The protein

Catalyzed reaction/ biological activity

  • control of the threonine biosynthetic genes (hom-thrC-thrB and thrD) PubMed
  • Protein family

  • UPF0735 family (according to Swiss-Prot)
  • Domains

  • putative DNA binding signature (aa 19-51)
  • ACT domain (aa 70 ... 145) (according to the Interpro database)
  • Effectors of protein activity

  • lysine and cysteine (indirectly) inhibit DNA-binding activity of ThrR PubMed
  • Expression and Regulation

    Operons

    Description

    Sigma factors

  • SigA: sigma factor, PubMed, in SigA regulon
  • Additional information

  • expression is repressed by binding of RpoE to the A-rich sequence in the -35 region of the promoter PubMed
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    Biological materials

    Mutant

  • BKE27910 (thrR::erm, available in the BGSC and in Jrg Stlke's and Fabian Commichau's labs) PubMed
  • BKE27910 (thrR::erm trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATTTGCATCCCCCCTTTAA, downstream forward: _UP4_GGTGCATAAGGGAGAGAAAA
  • BKK27910 (thrR::kan trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATTTGCATCCCCCCTTTAA, downstream forward: _UP4_GGTGCATAAGGGAGAGAAAA
  • Expression vectors

  • pBP323 (N-terminal Strep-tag, in pGP172) (available in Fabian Commichau's lab) PubMed
  • pBP620 (N-terminal Strep-tag, for SPINE, purification from B. subtilis, in pGP380) (available in Fabian Commichau's lab) PubMed
  • pBP622 (C-terminal Strep-tag, for SPINE, purification from B. subtilis, in pGP382) (available in Fabian Commichau's lab) PubMed
  • Two-hybrid system

  • B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Fabian Commichau's lab PubMed
  • References

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