dipZ:Quickview: Difference between revisions

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{{Tab On|Quickview|dsbD}}{{Tab|Gene|dsbD}}{{Tab|Gene Product(s)|dsbD}}{{Tab|Expression|dsbD}}{{Tab|Evolution|dsbD}}{{Tab|On One Page|dsbD}}{{TabsBottom}}
{{Tab On|Quickview|dipZ}}{{Tab|Gene|dipZ}}{{Tab|Gene Product(s)|dipZ}}{{Tab|Expression|dipZ}}{{Tab|Evolution|dipZ}}{{Tab|On One Page|dipZ}}{{TabsBottom}}
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!align=left {{table_heading_style}} |Standard Name
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''dsbD''
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!align=left {{table_heading_style}} |Gene Synonym(s)
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''dipZ, ECK4130, b4136, JW5734, cutA2, cycZ, htrI'', dsbD<ref name='LIB:Riley_2006'/><ref name='LIB:EcoCyc10.6'/>, htrI''
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!align=left {{table_heading_style}} |Product Desc.
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fused thiol:disulfide interchange protein<ref name='PMID:7628442'/>: membrane electron transporter<ref name='PMID:8917542'/>: activator of DsbC<ref name='LIB:Riley_2006'/>
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!{{table_heading_style}} |Gene Name
!align=left {{table_heading_style}} |Product Synonyms(s)
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[[dsbD:Gene|''dsbD]]'' (synonyms: ''dipZ, ECK4130, b4136, JW5734, cutA2, cycZ, htrI'')<ref name='LIB:Riley_2006'/><ref name='LIB:EcoCyc10.6'/>
''B4136<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, HtrI<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, CycZ<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, DipZ, cutA2, cycZ, dipZ, ECK4130, htrI, JW5734, b4136''
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!{{table_heading_style}} |Product(s)
!align=left {{table_heading_style}} |Function from GO
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[[dsbD:Gene_Product(s)|DipZ product, DipZ product]]<ref name='LIB:Riley_2006'/><ref name='LIB:EcoCyc10.6'/>: fused thiol:disulfide interchange protein: activator of DsbC<ref name='LIB:Riley_2006'/>, conserved protein<ref name='LIB:Riley_2006'/>, B4136<ref name='LIB:EcoCyc10.6'/>, HtrI<ref name='LIB:EcoCyc10.6'/>, DipZ<ref name='LIB:EcoCyc10.6'/>, CycZ<ref name='LIB:EcoCyc10.6'/>, DsbD<ref name='LIB:EcoCyc10.6'/>
<GO_nr />
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!{{table_heading_style}} |Description
!align=left {{table_heading_style}} |Knock-Out Phenotype
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DsbD<SUB>reduced</SUB><ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>
copper sensitivity PMID:8917542 PMID:16087673: temperature sensitivity PMID:7628442
 
 
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!{{table_heading_style}} |Knock-Out Phenotype
!align=left {{table_heading_style}} |Regulation/Expression
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!align=left {{table_heading_style}} |Regulation/Activity
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transcription unit(s): [[:Category:txn_units:yjdC|yjdC]]<ref name='LIB:EcoCyc10.6'/>
The bacterial membrane protein DsbD transfers electrons across the cytoplasmic membrane to reduce protein disulfide bonds in extracytoplasmic proteins. Its substrates include protein disulfide isomerases and a protein involved in cytochrome c assembly. It has three domains, each containing two redox-active cysteines. Electrons are transferred between them through thiol-disulfide exchange reactions.  
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!{{table_heading_style}} |Regulation/Activity
!align=left {{table_heading_style}} |Quick Links
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[[File:porteco.png|link=http://porteco.org/AjaxSearch.jsp?searchString=dipZ&s=search]] [[File:EcoCyc.gif|link=http://biocyc.org/ECOLI/NEW-IMAGE?type=NIL&object=EG12178]] [[File:regulondb.jpg|link=http://regulondb.ccg.unam.mx/gene?term=ECK120002071&organism=ECK12&format=jsp&type=gene ]] <br/><br/> [[File:dnadisplay.png|link=http://ecoliwiki.net/tools/display_dna.php?gene=dipZ&loc=MG1655%3A4363065..4361368,W3110%3A4369720..4368023,DH10B%3A4463427..4461730,REL606%3A4343763..4342066,BW2952%3A4300103..4301800]] [[File:proteindisplay.png|link=http://ecoliwiki.net/tools/display_protein.php?f=NC_000913&start=4300103&end=4301800&gene=dipZ&aa=maqriftlilllcstsvfaglfdapgrsqfvpadqafafdfqqnqhdlnltwqikdgyylyrkqiritpehakiadvqlpqgvwhedefygkseiyrdrltlpvtinqasagatltvtyqgcadagfcyppetktvplsevvannaapqpvsvpqqeqptaqlpfsalwalligigiaftpcvlpmyplisgivlggkqrlstarallltfiyvqgmaltytalglvvaaaglqfqaalqhpyvliglaivftllamsmfglftlqlpsslqtrltlmsnrqqggspggvfvmgaiaglicspcttaplsaillyiaqsgnmwlgggtlylyalgmglplmlitvfgnrllpksgpwmeqvktafgfvilalpvfllervigdvwglrlwsalgvaffgwafitslqakrgwmrivqiillaaalvsvrplqdwafgathtaqtqthlnftqiktvdelnqalveakgkpvmldlyadwcvackefekytfsdpqvqkaladtvllqanvtandaqdvallkhlnvlglptilffdgqgqehpqarvtgfmdaetfsahlrdrqp]]&nbsp;&nbsp;  [[File:pubmed.jpg|link=http://www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=Search&Term=dipZ+AND+escherichia+coli]]&nbsp;&nbsp;  [[File:textpresso.jpg|link=http://textpresso.tamu.edu/cgi-bin/textpresso/search?q=dipZ]]&nbsp;&nbsp;


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==Notes==
===Notes===
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==References==
==References==
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Latest revision as of 21:58, 27 May 2013

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

dsbD

Gene Synonym(s)

dipZ, ECK4130, b4136, JW5734, cutA2, cycZ, htrI, dsbD[1][2], htrI

Product Desc.

fused thiol:disulfide interchange protein[3]: membrane electron transporter[4]: activator of DsbC[1]

Product Synonyms(s)

B4136[2][1], HtrI[2][1], CycZ[2][1], DipZ, cutA2, cycZ, dipZ, ECK4130, htrI, JW5734, b4136

Function from GO

<GO_nr />

Knock-Out Phenotype

copper sensitivity PMID:8917542[4] PMID:16087673[5]: temperature sensitivity PMID:7628442[3]

Regulation/Expression
Regulation/Activity

The bacterial membrane protein DsbD transfers electrons across the cytoplasmic membrane to reduce protein disulfide bonds in extracytoplasmic proteins. Its substrates include protein disulfide isomerases and a protein involved in cytochrome c assembly. It has three domains, each containing two redox-active cysteines. Electrons are transferred between them through thiol-disulfide exchange reactions.

Quick Links



        

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Notes

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References

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  1. ↑ 1.0 1.1 1.2 1.3 1.4 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 Missiakas, D et al. (1995) Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14 3415-24 PubMed
  4. ↑ 4.0 4.1 Rietsch, A et al. (1996) An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 93 13048-53 PubMed
  5. ↑ Hiniker, A et al. (2005) Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. J. Biol. Chem. 280 33785-91 PubMed
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