dipZ:Quickview: Difference between revisions

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!align=left {{table_heading_style}} |Standard Name
!align=left |Standard Name
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''dsbD''  
''dsbD''  
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!align=left {{table_heading_style}} |Gene Synonym(s)
!align=left |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'/>
''dipZ, ECK4130, b4136, JW5734, cutA2, cycZ, htrI'', dsbD<ref name='LIB:Riley_2006'/><ref name='LIB:EcoCyc10.6'/>
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!align=left {{table_heading_style}} |Product Desc.
!align=left |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'/>
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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!align=left {{table_heading_style}} |Product Synonyms(s)
!align=left |Product Synonyms(s)
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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
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
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!align=left {{table_heading_style}} |Knock-Out Phenotype
!align=left |Knock-Out Phenotype
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copper sensitivity PMID:8917542 PMID:16087673: temperature sensitivity PMID:7628442
copper sensitivity PMID:8917542 PMID:16087673: temperature sensitivity PMID:7628442
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!align=left {{table_heading_style}} |Regulation/Expression
!align=left |Regulation/Expression
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!align=left {{table_heading_style}} |Regulation/Activity
!align=left |Regulation/Activity
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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.  
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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Revision as of 00:38, 9 January 2010

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

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

Standard Name

dsbD

Gene Synonym(s)

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

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

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.

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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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