Difference between revisions of "ThdF"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[gidA]]'', ''[[jag]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[gidA]]'', ''[[jag]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU41020 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU41020 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU41020 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU41020 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU41020 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU41020 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:ThdF_jag_spoIIIJ_rnpA_rpmH_context.png]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:ThdF_jag_spoIIIJ_rnpA_rpmH_context.png]]

Revision as of 11:46, 14 May 2013

  • Description: GTP-binding protein, putative tRNA modification GTPase

Gene name thdF
Synonyms mnmE
Essential no
Product putative tRNA modification GTPase
Function tRNA modification
Gene expression levels in SubtiExpress: thdF
Interactions involving this protein in SubtInteract: ThdF
MW, pI 50 kDa, 4.643
Gene length, protein length 1377 bp, 459 aa
Immediate neighbours gidA, jag
Sequences Protein DNA DNA_with_flanks
Genetic context
ThdF jag spoIIIJ rnpA rpmH context.png
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ThdF expression.png















Categories containing this gene/protein

translation, GTP-binding proteins

This gene is a member of the following regulons

ComK regulon

The gene

Basic information

  • Locus tag: BSU41020

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Binds and hydrolyzes GTP and readily exchanges GDP for GTP
  • Protein family: MnmE subfamily (according to Swiss-Prot) Era/Obg family

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Information on the corresponding protein from E. coli: EcoCyc MnmE required for wild-type 5-methylaminomethyl-2-thiouridine modification of tRNA, interacts with GidA. MnmE also appears to play a role in oxidation of thiophene and furan compounds and regulates glutamate-dependent acid resistance.

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Naotake Ogasawara, Nara, Japan

Your additional remarks

References

Reviews

Original publications

Silvia Prado, Magda Villarroya, Milagros Medina, M-Eugenia Armengod
The tRNA-modifying function of MnmE is controlled by post-hydrolysis steps of its GTPase cycle.
Nucleic Acids Res: 2013, 41(12);6190-208
[PubMed:23630314] [WorldCat.org] [DOI] (I p)

Takuya Morimoto, Pek Chin Loh, Tomohiro Hirai, Kei Asai, Kazuo Kobayashi, Shigeki Moriya, Naotake Ogasawara
Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis.
Microbiology (Reading): 2002, 148(Pt 11);3539-3552
[PubMed:12427945] [WorldCat.org] [DOI] (P p)

Mitsuo Ogura, Hirotake Yamaguchi, Kazuo Kobayashi, Naotake Ogasawara, Yasutaro Fujita, Teruo Tanaka
Whole-genome analysis of genes regulated by the Bacillus subtilis competence transcription factor ComK.
J Bacteriol: 2002, 184(9);2344-51
[PubMed:11948146] [WorldCat.org] [DOI] (P p)

Jörg Sievers, Brian Raether, Marta Perego, Jeff Errington
Characterization of the parB-like yyaA gene of Bacillus subtilis.
J Bacteriol: 2002, 184(4);1102-11
[PubMed:11807071] [WorldCat.org] [DOI] (P p)