Difference between revisions of "CitM"

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=The gene=
 
=The gene=

Revision as of 14:59, 22 June 2009

  • Description: Mg2+-citrate transporter

Gene name citM
Synonyms yflO
Essential no
Product Mg2+-citrate transporter
Function citrate uptake
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 45 kDa, 6.227
Gene length, protein length 1299 bp, 433 aa
Immediate neighbours yflP, yflN
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
CitM context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU07610

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: View classification (according to Swiss-Prot)
  • Paralogous protein(s): CitH

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation: repressed by glucose (CcpA)
  • Regulatory mechanism: CcpA: transcription repression
  • 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

Guillermo D Repizo, Víctor S Blancato, Pablo D Sender, Juke Lolkema, Christian Magni
Catabolite repression of the citST two-component system in Bacillus subtilis.
FEMS Microbiol Lett: 2006, 260(2);224-31
[PubMed:16842348] [WorldCat.org] [DOI] (P p)

Jessica B Warner, Juke S Lolkema
A Crh-specific function in carbon catabolite repression in Bacillus subtilis.
FEMS Microbiol Lett: 2003, 220(2);277-80
[PubMed:12670692] [WorldCat.org] [DOI] (P p)

Jessica B Warner, Christian Magni, Juke S Lolkema
CcpA-independent regulation of expression of the Mg2+ -citrate transporter gene citM by arginine metabolism in Bacillus subtilis.
J Bacteriol: 2003, 185(3);854-9
[PubMed:12533460] [WorldCat.org] [DOI] (P p)

Jessica B Warner, Juke S Lolkema
Growth of Bacillus subtilis on citrate and isocitrate is supported by the Mg2+-citrate transporter CitM.
Microbiology (Reading): 2002, 148(Pt 11);3405-3412
[PubMed:12427932] [WorldCat.org] [DOI] (P p)

Bastiaan P Krom, Henry Huttinga, Jessica B Warner, Juke S Lolkema
Impact of the Mg(2+)-citrate transporter CitM on heavy metal toxicity in Bacillus subtilis.
Arch Microbiol: 2002, 178(5);370-5
[PubMed:12375105] [WorldCat.org] [DOI] (P p)

H Li, A M Pajor
Functional characterization of CitM, the Mg2+-citrate transporter.
J Membr Biol: 2002, 185(1);9-16
[PubMed:11891560] [WorldCat.org] [DOI] (P p)

B P Krom, J B Warner, W N Konings, J S Lolkema
Complementary metal ion specificity of the metal-citrate transporters CitM and CitH of Bacillus subtilis.
J Bacteriol: 2000, 182(22);6374-81
[PubMed:11053381] [WorldCat.org] [DOI] (P p)

J B Warner, B P Krom, C Magni, W N Konings, J S Lolkema
Catabolite repression and induction of the Mg(2+)-citrate transporter CitM of Bacillus subtilis.
J Bacteriol: 2000, 182(21);6099-105
[PubMed:11029430] [WorldCat.org] [DOI] (P p)

H Yamamoto, M Murata, J Sekiguchi
The CitST two-component system regulates the expression of the Mg-citrate transporter in Bacillus subtilis.
Mol Microbiol: 2000, 37(4);898-912
[PubMed:10972810] [WorldCat.org] [DOI] (P p)

A Boorsma, M E van der Rest, J S Lolkema, W N Konings
Secondary transporters for citrate and the Mg(2+)-citrate complex in Bacillus subtilis are homologous proteins.
J Bacteriol: 1996, 178(21);6216-22
[PubMed:8892821] [WorldCat.org] [DOI] (P p)

P Carlsson, L Hederstedt
Bacillus subtilis citM, the structural gene for dihydrolipoamide transsuccinylase: cloning and expression in Escherichia coli.
Gene: 1987, 61(2);217-24
[PubMed:3127276] [WorldCat.org] [DOI] (P p)