pcrA [2019-04-12 13:51:33]

ATP-dependent DNA helicase, facilitates unwinding of ICEBs1 DNA for horizontal transfer

Locus: BSU06610

Isoelectric point: 5.77

Molecular weight: 83.37 kDa

Protein length: 739 aa

Gene length: 2220 bp

Function: plasmid rolling-circle replication, conjugative transfer of ICEBs1

Product: ATP-dependent DNA helicase

Essential: yes

Synonyms: yerF

Genomic Context

Loading

Categories containing this gene/protein

• Information processing → Genetics → DNA repair/ recombination
• Information processing → Genetics → DNA repair/ recombination → Other proteins
• Prophages and mobile genetic elements → Mobile genetic elements → Additional genes
• Groups of genes → Essential genes

Gene

Coordinates: 719,370 → 721,589

Phenotypes of a mutant

• essential PubMed

The protein

Catalyzed reaction/ biological activity

• PcrA anchors itself to the template duplex using the 2B subdomain and reels in the lagging strand, extruding a single-stranded loop PubMed
• dismantles RecA filaments PubMed

Protein family

• uvrD-like helicase C-terminal domain (according to Swiss-Prot)

Paralogous protein(s)

• YjcD

Domains

• two RecA-like domains PubMed
• intrinxically disordered C-terminal domain (for interaction with RNA polymerase) PubMed

Effectors of protein activity

• unwinding of the double-stranded ICEBs1 DNA is stimulated by HelP PubMed
• helicase activity is stimulated by interaction with RNA polymerase PubMed

Structure

• 2PJR (product complex, complex with sulphate ion, Geobacillus stearothermophilus)
• 1PJR (substrate complex, complex with DNA, Geobacillus stearothermophilus)
• 5DMA, C-terminal RNA polymerase interaction domain PubMed

Expression and Regulation

Operons

• Genes: pcrB-pcrA-ligA-yerH
  Description: PubMed

  Regulatory mechanism

  • LexA: repression, PubMed, in LexA regulon

  Regulation

  • induced by DNA damage (LexA) PubMed

Biological materials

Two-hybrid system

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

References

Reviews

Loading

Original Publications

Loading