umuD:Quickview: Difference between revisions

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{{Tab On|Quickview|umuD}}{{Tab|Gene|umuD}}{{Tab|Gene Product(s)|umuD}}{{Tab|Expression|umuD}}{{Tab|Evolution|umuD}}{{Tab|On One Page|umuD}}{{TabsBottom}}
{{Tab On|Quickview|umuD}}{{Tab|Gene|umuD}}{{Tab|Gene Product(s)|umuD}}{{Tab|Expression|umuD}}{{Tab|Evolution|umuD}}{{Tab|On One Page|umuD}}{{TabsBottom}}
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!{{table_heading_style}} |Gene Name
!align=left {{table_heading_style}} |Standard Name
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[[umuD:Gene|''umuD]]'' (synonyms: ''ECK1171, b1183, JW1172, uvm'')<ref name='LIB:Riley_2006'/>
''umuD''
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!{{table_heading_style}} |Product(s)  
!align=left {{table_heading_style}} |Gene Synonym(s)
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[[umuD:Gene_Product(s)|UmuD product]]<ref name='LIB:Riley_2006'/>: DNA polymerase V, subunit D<ref name='LIB:Riley_2006'/>, B1183<ref name='LIB:EcoCyc10.6'/>, UmuD<ref name='LIB:EcoCyc10.6'/>, [[:Category:Complex:DNA polymerase V|DNA polymerase V]]<ref name='LIB:EcoCyc11.1'/>
''ECK1171, b1183, JW1172, uvm''<ref name='LIB:Riley_2006'/>
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!{{table_heading_style}} |Description
!align=left {{table_heading_style}} |Product Desc.
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SOS mutagenesis; error-prone repair; processed to UmuD'; forms complex with UmuC<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>
SOS mutagenesis; error-prone repair; processed to UmuD'; forms complex with UmuC<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;


Component of [[:Category:Complex:DNA polymerase V|DNA polymerase V]]<ref name='LIB:EcoCyc11.1'/>


DNA polymerase V subunit, capable of translesion synthesis; inducible mutagenesis; error-prone repair; UmuDC single-stranded binding protein with RecA-coated DNA; intrinsic AP lyase activity<ref name='LIB:EcoGene'/>
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!align=left {{table_heading_style}} |Product Synonyms(s)
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''DNA polymerase V, subunit D<ref name='LIB:Riley_2006'/>, B1183<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, UmuD<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/> , ECK1171, JW1172, b1183''
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!align=left {{table_heading_style}} |Function from GO
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<GO_nr />
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!{{table_heading_style}} |Knock-Out Phenotype
!align=left {{table_heading_style}} |Knock-Out Phenotype
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!{{table_heading_style}} |Regulation/Expression
!align=left {{table_heading_style}} |Regulation/Expression
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transcription unit(s): [[:Category:txn_units:umuDC|umuDC]]<ref name='LIB:EcoCyc10.6'/>, OP00250  
transcription unit(s): [[:Category:Txn_unit:umuDC|umuDC]]<ref name='LIB:EcoCyc10.6'/>, OP00250  
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!{{table_heading_style}} |Regulation/Activity
!align=left {{table_heading_style}} |Regulation/Activity
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!align=left {{table_heading_style}} |Quick Links
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[[File:porteco.png|link=http://porteco.org/AjaxSearch.jsp?searchString=umuD&s=search]] [[File:EcoCyc.gif|link=http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=EG11057]] [[File:regulondb.jpg|link=http://regulondb.ccg.unam.mx/gene?term=ECK120001046&organism=ECK12&format=jsp&type=gene ]] <br/><br/> [[File:dnadisplay.png|link=http://ecoliwiki.net/tools/display_dna.php?gene=umuD&loc=MG1655%3A1229990..1230409,W3110%3A1232344..1232763,DH10B%3A1270231..1270650,REL606%3A1230917..1231336,BW2952%3A1118711..1119130]] [[File:proteindisplay.png|link=http://ecoliwiki.net/tools/display_protein.php?f=NC_000913&start=1118711&end=1119130&gene=umuD&aa=mlfikpadlreivtfplfsdlvqcgfpspaadyveqridlnqlliqhpsatyfvkasgdsmidggisdgdllivdsaitashgdiviaavdgeftvkklqlrptvqlipmnsayspitissedtldvfgvvihvvkamr]]&nbsp;&nbsp;  [[File:pubmed.jpg|link=http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Search&Term=umuD+AND+escherichia+coli]]&nbsp;&nbsp;  [[File:textpresso.jpg|link=http://textpresso.tamu.edu/cgi-bin/textpresso/search?q=umuD]]&nbsp;&nbsp;
 
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==Notes==
===Notes===
{{BacktoTop}}
 
LexA regulon. Autocleavage removes the first 24 amino acids to form UmuD', required for mutageneic translesion synthesis (TLS). UmuD and UmuD' are intrinsically disordered proteins (IDPs) that can nonetheless form stable dimers (Simon, 2008)<ref name='PMID:18216271'/>.<ref name='LIB:EcoGene'/> A monomeric variant of UmuD has been identified that is active for cleavage to form UmuD' and for other functions <ref name='PMID:21118802'/>.
 




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==References==
==References==
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Latest revision as of 21:45, 27 May 2013

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Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
References Suggestions
Standard Name

umuD

Gene Synonym(s)

ECK1171, b1183, JW1172, uvm[1]

Product Desc.

SOS mutagenesis; error-prone repair; processed to UmuD'; forms complex with UmuC[2][3];

Component of DNA polymerase V[3]

DNA polymerase V subunit, capable of translesion synthesis; inducible mutagenesis; error-prone repair; UmuDC single-stranded binding protein with RecA-coated DNA; intrinsic AP lyase activity[4]

Product Synonyms(s)

DNA polymerase V, subunit D[1], B1183[2][1], UmuD[2][1] , ECK1171, JW1172, b1183

Function from GO

<GO_nr />

Knock-Out Phenotype
Regulation/Expression

transcription unit(s): umuDC[2], OP00250

Regulation/Activity
Quick Links



        

See Help:Quickview for help with entering information in the Quickview table.

Notes

[back to top]


LexA regulon. Autocleavage removes the first 24 amino acids to form UmuD', required for mutageneic translesion synthesis (TLS). UmuD and UmuD' are intrinsically disordered proteins (IDPs) that can nonetheless form stable dimers (Simon, 2008)[5].[4] A monomeric variant of UmuD has been identified that is active for cleavage to form UmuD' and for other functions [6].



References

[back to top]


  1. ↑ 1.0 1.1 1.2 1.3 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ 4.0 4.1 EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ Simon, SM et al. (2008) Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products. Proc. Natl. Acad. Sci. U.S.A. 105 1152-7 PubMed
  6. ↑ Ollivierre, JN et al. (2011) The dimeric SOS mutagenesis protein UmuD is active as a monomer. J. Biol. Chem. 286 3607-17 PubMed