MetE

• Description: methionine synthase
  
  

Gene name	metE
Synonyms	metC
Essential	no
Product	methionine synthase
Function	biosynthesis of methionine
Gene expression levels in SubtiExpress: metE
Metabolic function and regulation of this protein in SubtiPathways: Cys, Met & Sulfate assimilation
MW, pI	86 kDa, 4.839
Gene length, protein length	2286 bp, 762 aa
Immediate neighbours	guaD, ispA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, phosphoproteins

This gene is a member of the following regulons

S-box

The gene

Basic information

• Locus tag: BSU13180

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine (according to Swiss-Prot)

• Protein family: vitamin-B12 independent methionine synthase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on ser/ thr/ tyr PubMed, S-cysteinylation after diamide stress (C719) PubMed
  • Cys719 and Cys730 are S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species PubMed PubMed
  • MetE is generally most strongly S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species PubMed PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 1T7L (from Thermotoga maritima, 44% identity, 61% similarity) PubMed

• UniProt: P80877

• KEGG entry: [2]

• E.C. number: 2.1.1.14

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon: metE

• Expression browser: metE PubMed

• Sigma factor:

• Regulation:
  • repressed by casamino acids PubMed
  • repressed by methionine (about 1000-fold)(S-box) PubMed

• Regulatory mechanism: S-box: transcription termination/ antitermination, the S-box riboswitch binds S-adenosylmethionine resulting in termination PubMed

• Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

• Mutant:
  • 1A607 ( metE::erm), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Ahmed Gaballa, Bui Khanh Chi, Alexandra A Roberts, Dörte Becher, Chris J Hamilton, Haike Antelmann, John D Helmann
Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and BrxB(YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and MetE.
Antioxid Redox Signal: 2014, 21(3);357-67
[PubMed:24313874] [WorldCat.org] [DOI] (I p)

Bui Khanh Chi, Alexandra A Roberts, Tran Thi Thanh Huyen, Katrin Bäsell, Dörte Becher, Dirk Albrecht, Chris J Hamilton, Haike Antelmann
S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.
Antioxid Redox Signal: 2013, 18(11);1273-95
[PubMed:22938038] [WorldCat.org] [DOI] (I p)

Bui Khanh Chi, Katrin Gronau, Ulrike Mäder, Bernd Hessling, Dörte Becher, Haike Antelmann
S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics.
Mol Cell Proteomics: 2011, 10(11);M111.009506
[PubMed:21749987] [WorldCat.org] [DOI] (I p)

Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532] [WorldCat.org] [DOI] (I p)

Jerneja Tomsic, Brooke A McDaniel, Frank J Grundy, Tina M Henkin
Natural variability in S-adenosylmethionine (SAM)-dependent riboswitches: S-box elements in bacillus subtilis exhibit differential sensitivity to SAM In vivo and in vitro.
J Bacteriol: 2008, 190(3);823-33
[PubMed:18039762] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Falko Hochgräfe, Jörg Mostertz, Dierk-Christoph Pöther, Dörte Becher, John D Helmann, Michael Hecker
S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.
J Biol Chem: 2007, 282(36);25981-5
[PubMed:17611193] [WorldCat.org] [DOI] (P p)

Falko Hochgräfe, Jörg Mostertz, Dirk Albrecht, Michael Hecker
Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis.
Mol Microbiol: 2005, 58(2);409-25
[PubMed:16194229] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

F J Grundy, T M Henkin
The S box regulon: a new global transcription termination control system for methionine and cysteine biosynthesis genes in gram-positive bacteria.
Mol Microbiol: 1998, 30(4);737-49
[PubMed:10094622] [WorldCat.org] [DOI] (P p)