Difference between revisions of "InfB"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ylxQ]]'', ''[[ylxP]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ylxQ]]'', ''[[ylxP]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU16630 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU16630 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU16630 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU16630 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU16630 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU16630 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:infB_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:infB_context.gif]]

Revision as of 10:16, 14 May 2013

  • Description: translation initiation factor IF-2

Gene name infB
Synonyms
Essential yes PubMed
Product initiation factor IF-2
Function translation
Gene expression levels in SubtiExpress: infB
MW, pI 78 kDa, 5.191
Gene length, protein length 2148 bp, 716 aa
Immediate neighbours ylxQ, ylxP
Sequences Protein DNA DNA_with_flanks
Genetic context
InfB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
InfB expression.png
























Categories containing this gene/protein

translation, essential genes

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU16630

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: Initiation of translation
  • Protein family: IF-2 family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains: Nucleotide-binding domain that competitively binds GTP or ppGpp PubMed
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity: GTP and ppGpp PubMed

Database entries

  • Structure: 1D1N (fMet-tRNA-fMet binding domain, Geobacillus stearothermophilus), 1Z9B (C1-subdomain, Geobacillus stearothermophilus)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
    • Interaction with ppGpp interferes with IF2-dependent initiation complex formation, severely inhibits initiation dipeptide formation, and blocks the initiation step of translation.PubMed
  • Regulatory mechanism:
  • Additional information: Putative cellular metabolic sensor and regulator that oscillates between an active GTP-bound form under conditions allowing active protein syntheses and an inactive ppGpp-bound form when depleting of nutrients PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Pohl Milon, Eugene Tischenko, Jerneja Tomsic, Enrico Caserta, Gert Folkers, Anna La Teana, Marina V Rodnina, Cynthia L Pon, Rolf Boelens, Claudio O Gualerzi
The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor.
Proc Natl Acad Sci U S A: 2006, 103(38);13962-7
[PubMed:16968770] [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)

K Shazand, J Tucker, M Grunberg-Manago, J C Rabinowitz, T Leighton
Similar organization of the nusA-infB operon in Bacillus subtilis and Escherichia coli.
J Bacteriol: 1993, 175(10);2880-7
[PubMed:8491709] [WorldCat.org] [DOI] (P p)