Difference between revisions of "RacX"

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|style="background:#ABCDEF;" align="center"|'''Function''' || control of [[biofilm formation]]  
 
|style="background:#ABCDEF;" align="center"|'''Function''' || control of [[biofilm formation]]  
 
|-
 
|-
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU34430 racX]
+
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU34430 racX]
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 25 kDa, 5.396   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 25 kDa, 5.396   
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yveF]]'', ''[[pbpE]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yveF]]'', ''[[pbpE]]''
 
|-
 
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+&#91;EMBLCDS:CAB15448&#93;+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU34430 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU34430 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU34430 Advanced_DNA]
 
|-
 
|-
 
|colspan="2" | '''Genetic context''' <br/> [[Image:racX_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:racX_context.gif]]

Revision as of 13:55, 13 May 2013

  • Description: amino acid racemase, production of D-amino acids, control of biofilm formation

Gene name racX
Synonyms
Essential no
Product amino acid racemase
Function control of biofilm formation
Gene expression levels in SubtiExpress: racX
MW, pI 25 kDa, 5.396
Gene length, protein length 681 bp, 227 aa
Immediate neighbours yveF, pbpE
Sequences Protein DNA Advanced_DNA
Genetic context
RacX context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RacX expression.png
























Categories containing this gene/protein

biofilm formation, cell envelope stress proteins (controlled by SigM, V, W, X, Y)

This gene is a member of the following regulons

SigW regulon

The gene

Basic information

  • Locus tag: BSU34430

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: aspartate/glutamate racemases family (according to Swiss-Prot)
  • Paralogous protein(s):

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

Expression and regulation

  • 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

Ilana Kolodkin-Gal, Diego Romero, Shugeng Cao, Jon Clardy, Roberto Kolter, Richard Losick
D-amino acids trigger biofilm disassembly.
Science: 2010, 328(5978);627-9
[PubMed:20431016] [WorldCat.org] [DOI] (I p)

María Mercedes Palomino, Carmen Sanchez-Rivas, Sandra M Ruzal
High salt stress in Bacillus subtilis: involvement of PBP4* as a peptidoglycan hydrolase.
Res Microbiol: 2009, 160(2);117-24
[PubMed:19063962] [WorldCat.org] [DOI] (P p)

X Huang, A Gaballa, M Cao, J D Helmann
Identification of target promoters for the Bacillus subtilis extracytoplasmic function sigma factor, sigma W.
Mol Microbiol: 1999, 31(1);361-71
[PubMed:9987136] [WorldCat.org] [DOI] (P p)

M A Strauch
Delineation of AbrB-binding sites on the Bacillus subtilis spo0H, kinB, ftsAZ, and pbpE promoters and use of a derived homology to identify a previously unsuspected binding site in the bsuB1 methylase promote.
J Bacteriol: 1995, 177(23);6999-7002
[PubMed:7592498] [WorldCat.org] [DOI] (P p)

D L Popham, P Setlow
Cloning, nucleotide sequence, and regulation of the Bacillus subtilis pbpE operon, which codes for penicillin-binding protein 4* and an apparent amino acid racemase.
J Bacteriol: 1993, 175(10);2917-25
[PubMed:8491712] [WorldCat.org] [DOI] (P p)