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epsB [Tue Dec 13 2016 11:16:36 GMT+0100 (CET)]
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epsB [Tue Dec 13 2016 11:16:36 GMT+0100 (CET)]

extracellular polysaccharide synthesis, protein tyrosine kinase
locus
BSU34360
pI
9.92
mw
24.00 kDa
function
biofilm formation
product
protein tyrosine kinase
essential
no
synonyms
yveL

Genomic Context

      

categories

  • [category|SW 3|Information processing] → [category|SW 3.3|Protein synthesis, modification and degradation] → [category|SW 3.3.4|Protein modification] → [category|SW 3.3.4.2|Protein kinases]
  • [category|SW 4|Lifestyles] → [category|SW 4.1|Exponential and early post-exponential lifestyles] → [category|SW 4.1.2|Biofilm formation]
  • [category|SW 4|Lifestyles] → [category|SW 4.1|Exponential and early post-exponential lifestyles] → [category|SW 4.1.2|Biofilm formation] → [category|SW 4.1.2.1|Matrix polysaccharide synthesis]
  • [category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.7|Phosphorylation on a Tyr residue]
  • [SW|Categories] containing this gene/protein

  • [SW|protein modification], [SW|biofilm formation], [SW|phosphoproteins]
  • This gene is a member of the following [SW|regulons]

  • [SW|AbrB regulon], [SW|RemA regulon], [SW|SinR regulon]
  • Gene

    Coordinates on the chromosome (coding sequence)
    3,528,462 -> 3,529,145

    The protein

    Catalyzed reaction/ biological activity

  • ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate (according to Swiss-Prot)
  • Protein family

  • BY kinase, see the [http://bykdb.ibcp.fr/BYKdb/BYKdbHelp Bacterial Protein Tyrosine Kinase Database])
  • Paralogous protein(s)

  • [protein|search|PtkA]
  • Modification

  • autophosphorylated on Tyr-225 and Tyr-227 [Pubmed|25085422]
  • Structure

  • [PDB|2VED] (CapB, the homolog in ''Staphylococcus aureus'') [Pubmed|18547145]
  • [SW|Interactions]

  • [protein|search|EpsA]-[protein|search|EpsB] [Pubmed|24493247]
  • Expression and Regulation

    Operon

  • ''[protein|search|epsA]-[protein|search|epsB]-[protein|search|epsC]-[protein|search|epsD]-[protein|search|epsE]-[protein|search|epsF]-[protein|search|epsG]-[protein|search|epsH]-[protein|search|epsI]-[protein|search|epsJ]-[protein|search|epsK]-[protein|search|epsL]-[protein|search|epsM]-[protein|search|epsN]-[protein|search|epsO]'' [Pubmed|15661000]
  • [SW|Sigma factor]

  • [protein|search|SigA] [Pubmed|15661000]
  • Regulation

  • repressed by [protein|search|SinR] [Pubmed|15661000]
  • Regulatory mechanism

  • [protein|search|SinR]: transcription anti-activation (prevents binding of [protein|search|RemA]) [Pubmed|23646920]
  • [protein|search|RemA]: transcription activation [Pubmed|23646920]
  • [protein|search|AbrB]: transcription repression [Pubmed|20817675]
  • Additional information

  • induction by sequestration of [protein|search|SinR] by [protein|search|SinI] or [protein|search|SlrA] [PubMed|15661000,19788541]
  • the '[protein|search|epsA]-[protein|search|epsB]-[protein|search|epsC]-[protein|search|epsD]-[protein|search|epsE]-[protein|search|epsF]-[protein|search|epsG]-[protein|search|epsH]-[protein|search|epsI]-[protein|search|epsJ]-[protein|search|epsK]-[protein|search|epsL]-[protein|search|epsM]-[protein|search|epsN]-[protein|search|epsO]' operon is not expressed in a '[protein|search|ymdB]' mutant [PubMed|21856853]
  • the amount of the mRNA is substantially decreased upon depletion of [Rny|search|RNase Y] (this is likely due to the increased stability of the '[protein|search|sinR]' mRNA) [PubMed|21815947]
  • Biological materials

    Mutant

  • GP1518 (aphA3) [Pubmed|24493247], available in [SW| Jörg Stülke]'s lab
  • GP1519 (''[protein|search|epsA]-[protein|search|epsB]'', aphA3) [Pubmed|24493247], available in [SW| Jörg Stülke]'s lab
  • two-hybrid system

  • B. pertussis adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]) [Pubmed|24493247], available in [SW| Jörg Stülke]'s lab
  • FLAG-tag construct

  • GP1541 epsB-FLAG 3x spc (based on [SW|pGP1331]) available in [SW| Jörg Stülke]'s lab
  • Antibody

  • **
  • Labs working on this gene/protein

  • [SW|Richard Losick], Harvard Univ., Cambridge, USA [http://www.mcb.harvard.edu/Losick/ homepage]
  • References

    Reviews

  • 20735481,24554699,25540643
  • Original publications

  • 15661000,16430695,18047568,18647168,18547145,20817675,21856853,21815947,23646920,24493247,24728941,25085422