Difference between revisions of "PcrA"

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=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:'''  
+
* '''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|20723756}}
 +
** dismantles [[RecA]] filaments {{PubMed|20723756}}
  
 
* '''Protein family:''' uvrD-like helicase C-terminal domain (according to Swiss-Prot)
 
* '''Protein family:''' uvrD-like helicase C-terminal domain (according to Swiss-Prot)
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<pubmed> 19943906 </pubmed>
 
<pubmed> 19943906 </pubmed>
 
==Original Publications==
 
==Original Publications==
<pubmed>12073041,9701819 ,16267290, 19943900 </pubmed>
+
<pubmed>12073041,9701819 ,16267290, 19943900 20723756 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 19:49, 15 October 2010

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

Gene name pcrA
Synonyms yerF
Essential yes PubMed
Product ATP-dependent DNA helicase
Function plasmid rolling-circle replication, conjugative transfer of ICEBs1
MW, pI 83 kDa, 5.767
Gene length, protein length 2217 bp, 739 aa
Immediate neighbours pcrB, ligA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PcrA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU06610

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • 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):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:

Database entries

  • Structure: 2PJR (�product complex�, complex with sulphate ion, Geobacillus stearothermophilus), 1PJR (�substrate complex�, complex with DNA, Geobacillus stearothermophilus)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original Publications

Jeehae Park, Sua Myong, Anita Niedziela-Majka, Kyung Suk Lee, Jin Yu, Timothy M Lohman, Taekjip Ha
PcrA helicase dismantles RecA filaments by reeling in DNA in uniform steps.
Cell: 2010, 142(4);544-55
[PubMed:20723756] [WorldCat.org] [DOI] (I p)

Catherine A Lee, Ana Babic, Alan D Grossman
Autonomous plasmid-like replication of a conjugative transposon.
Mol Microbiol: 2010, 75(2);268-79
[PubMed:19943900] [WorldCat.org] [DOI] (I p)

Nora Au, Elke Kuester-Schoeck, Veena Mandava, Laura E Bothwell, Susan P Canny, Karen Chachu, Sierra A Colavito, Shakierah N Fuller, Eli S Groban, Laura A Hensley, Theresa C O'Brien, Amish Shah, Jessica T Tierney, Louise L Tomm, Thomas M O'Gara, Alexi I Goranov, Alan D Grossman, Charles M Lovett
Genetic composition of the Bacillus subtilis SOS system.
J Bacteriol: 2005, 187(22);7655-66
[PubMed:16267290] [WorldCat.org] [DOI] (P p)

M-F Noirot-Gros, P Soultanas, D B Wigley, S D Ehrlich, P Noirot, M-A Petit
The beta-propeller protein YxaL increases the processivity of the PcrA helicase.
Mol Genet Genomics: 2002, 267(3);391-400
[PubMed:12073041] [WorldCat.org] [DOI] (P p)

M A Petit, E Dervyn, M Rose, K D Entian, S McGovern, S D Ehrlich, C Bruand
PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication.
Mol Microbiol: 1998, 29(1);261-73
[PubMed:9701819] [WorldCat.org] [DOI] (P p)