dppA:Quickview: Difference between revisions

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!align=left {{table_heading_style}} |Function from GO
!align=left {{table_heading_style}} |Function from GO
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'''Biological Process'''
<GO_nr />
* GO:0006857 oligopeptide transport ([http://www.geneontology.org/GO.evidence.shtml IGI])
* GO:0042938 dipeptide transport ([http://www.geneontology.org/GO.evidence.shtml IGI])
'''Molecular Function'''
* GO:0015198 oligopeptide transporter activity ([http://www.geneontology.org/GO.evidence.shtml IGI])
* GO:0015421 oligopeptide-transporting ATPase activity ([http://www.geneontology.org/GO.evidence.shtml ISS])
* GO:0042277 peptide binding ([http://www.geneontology.org/GO.evidence.shtml IDA])
* GO:0042936 dipeptide transporter activity ([http://www.geneontology.org/GO.evidence.shtml IGI])
'''Cellular Component'''
* GO:0043190 ATP-binding cassette (ABC) transporter complex ([http://www.geneontology.org/GO.evidence.shtml ISS])
 
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!align=left {{table_heading_style}} |Knock-Out Phenotype
!align=left {{table_heading_style}} |Knock-Out Phenotype

Revision as of 19:44, 2 February 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

dppA

Gene Synonym(s)

ECK3531, b3544, JW3513, alu, dpp, fpp[1]

Product Desc.

DppA[2][3];

Component of dipeptide ABC transporter[2][3]

Dipeptide/heme transport, periplasmic binding protein; recognition for transport and chemotaxis[4]

Product Synonyms(s)

dipeptide transporter[1], periplasmic-binding component of ABC superfamily[1], B3544[2][1], Fpp[2][1], Dpp[2][1], Alu[2][1], DppA[2][1]

Function from GO

<GO_nr />

Knock-Out Phenotype
Regulation/Expression

transcription unit(s): dppABCDF[2], dpp, dppABCDE

Regulation/Activity
Quick Links

DNA display    Protein display    Pubmed(dppA)    Textpresso(dppA)

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

Notes

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DppA binds dipeptides and heme, and mediates chemotaxis to dipeptides through the Tap chemoreceptor. E. coli does not normally use exogeneous heme, but heme can be utilized if a foreign OM heme receptor is expressed in E. coli; heme and dipeptides compete for the same binding site; MppA is an alternative heme periplasmic binding protein; MppA or DppA is required for the uptake of 5-aminolevulinic acid (Letoffe, 2006). After four hours of Zn(II) stress, DppA protein levels decreased (Easton, 2006).[4]



References

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  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 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 2.4 2.5 2.6 2.7 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.
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