Difference between revisions of "PnbA"

From SubtiWiki
Jump to: navigation, search
(Biological materials)
Line 85: Line 85:
 
=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1C7J 1C7J]
+
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1C7J 1C7J] {{PubMed|10535917}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37967 P37967]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P37967 P37967]
Line 131: Line 131:
 
=References=
 
=References=
  
<pubmed>7828905,21574267,17218307, </pubmed>
+
<pubmed>7828905,21574267,17218307, 10535917 22127613 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:18, 2 December 2011

  • Description: para-nitrobenzyl esterase

Gene name pnbA
Synonyms estB
Essential no
Product para-nitrobenzyl esterase
Function lipid degradation
MW, pI 53 kDa, 4.776
Gene length, protein length 1467 bp, 489 aa
Immediate neighbours slrR, padC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PnbA context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

utilization of lipids, phosphoproteins

This gene is a member of the following regulons

AbrB regulon

The gene

Basic information

  • Locus tag: BSU34390

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Triacylglycerol + H2O = diacylglycerol + a carboxylate (according to Swiss-Prot)
  • Protein family: type-B carboxylesterase/lipase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on Ser-189 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • repressed during logarithmic growth (AbrB) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
    • GP951 (pnbA::cat), available in Stülke lab
    • GP955 (slrR-pnbA::cat), available in Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Xiaozhen Yu, Sara C Sigler, Delwar Hossain, Monika Wierdl, Steven R Gwaltney, Philip M Potter, Randy M Wadkins
Global and local molecular dynamics of a bacterial carboxylesterase provide insight into its catalytic mechanism.
J Mol Model: 2012, 18(6);2869-83
[PubMed:22127613] [WorldCat.org] [DOI] (I p)

Doris Ribitsch, Sonja Heumann, Eva Trotscha, Enrique Herrero Acero, Katrin Greimel, Regina Leber, Ruth Birner-Gruenberger, Sigrid Deller, Inge Eiteljoerg, Peter Remler, Thomas Weber, Petra Siegert, Karl-Heinz Maurer, Ilaria Donelli, Giuliano Freddi, Helmut Schwab, Georg M Guebitz
Hydrolysis of polyethyleneterephthalate by p-nitrobenzylesterase from Bacillus subtilis.
Biotechnol Prog: 2011, 27(4);951-60
[PubMed:21574267] [WorldCat.org] [DOI] (I p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

B Spiller, A Gershenson, F H Arnold, R C Stevens
A structural view of evolutionary divergence.
Proc Natl Acad Sci U S A: 1999, 96(22);12305-10
[PubMed:10535917] [WorldCat.org] [DOI] (P p)

J Zock, C Cantwell, J Swartling, R Hodges, T Pohl, K Sutton, P Rosteck, D McGilvray, S Queener
The Bacillus subtilis pnbA gene encoding p-nitrobenzyl esterase: cloning, sequence and high-level expression in Escherichia coli.
Gene: 1994, 151(1-2);37-43
[PubMed:7828905] [WorldCat.org] [DOI] (P p)