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HigB-HigA DNA-binding transcriptional repressor

Synonyms: HigB-HigA
The crystal structure of the toxin-antitoxin (TA) HigBA complex has been resolved to 2.7 Å resolution. It displays a hetero-tetramer (HigBA)2 form comprised by two HigB and two HigA subunits [1]
HigA and HigBA autoregulate differentially in vivo. Helix-turn-helix (HTH) folds of (HigBA)2 are responsible for their recognition of operator DNA [1]

Transcription factor      
TF conformation(s):
Name Conformation Type TF-Effector Interaction Type Apo/Holo Conformation Evidence (Confirmed, Strong, Weak) References
HigB-HigA     nd nd
Connectivity class: Local Regulator
Gene name: higA
  Genome position: 3233728-3234144
  Length: 417 bp / 138 aa
Operon name: higBA
TU(s) encoding the TF:
Transcription unit        Promoter

Regulated gene(s) higA, higB
Multifun term(s) of regulated gene(s) MultiFun Term (List of genes associated to the multifun term)
transcriptional level (1)
translation attenuation and efficiency (1)
Regulated operon(s) higBA
First gene in the operon(s) higB
Simple and complex regulons HigA,HigB-HigA
Simple and complex regulatory phrases Regulatory phrase (List of promoters regulated by the phrase)

Transcription factor binding sites (TFBSs) arrangements       

  Functional conformation Function Promoter Sigma factor Central Rel-Pos Distance to first Gene Genes Sequence LeftPos RightPos Evidence (Confirmed, Strong, Weak) References
  HigB-HigA repressor higBp Sigma70 -27.0 -52.0 higB, higA
3234494 3234520 [BPP], [IHBCE] [1]
  HigB-HigA repressor higBp Sigma70 5.0 -21.0 higB, higA
3234467 3234485 [BPP], [IHBCE] [1]

Evolutionary conservation of regulatory elements    
     Note: Evolutionary conservation of regulatory interactions and promoters is limited to gammaproteobacteria.
Promoter-target gene evolutionary conservation


 [BPP] Binding of purified proteins

 [IHBCE] Inferred by a human based on computational evidence


 [1] Yang J., Zhou K., Liu P., Dong Y., Gao Z., Zhang J., Liu Q., 2016, Structural insight into the E.¿¿coli HigBA complex., Biochem Biophys Res Commun. 478(4):1521-7