Difference between revisions of "YrvO"

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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:'''
+
* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?structureId=1EG5 1EG5] (from Thermotoga maritima, 37% identity, 54% similarity) {{PubMed|10715213}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O34599 O34599]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O34599 O34599]
Line 120: Line 120:
  
 
=References=
 
=References=
<pubmed>16885442 11948165 </pubmed>
+
<pubmed>16885442 11948165 10715213 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:21, 3 February 2010

  • Description: similar to NifS protein homolog

Gene name yrvO
Synonyms nifS
Essential yes PubMed
Product unknown
Function unknown
MW, pI 41 kDa, 5.463
Gene length, protein length 1137 bp, 379 aa
Immediate neighbours trmU, cymR
Gene sequence (+200bp) Protein sequence
Genetic context
YrvO context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU27510

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • Structure: 1EG5 (from Thermotoga maritima, 37% identity, 54% similarity) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Soon-Yong Choi, Dindo Reyes, Montira Leelakriangsak, Peter Zuber
The global regulator Spx functions in the control of organosulfur metabolism in Bacillus subtilis.
J Bacteriol: 2006, 188(16);5741-51
[PubMed:16885442] [WorldCat.org] [DOI] (P p)

Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165] [WorldCat.org] [DOI] (P p)

J T Kaiser, T Clausen, G P Bourenkow, H D Bartunik, S Steinbacher, R Huber
Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly.
J Mol Biol: 2000, 297(2);451-64
[PubMed:10715213] [WorldCat.org] [DOI] (P p)