AbnA

From SubtiWiki
Revision as of 10:57, 14 May 2013 by 134.76.70.252 (talk)
Jump to: navigation, search
  • Description: endo-1,5-alpha-L-arabinosidase

Gene name abnA
Synonyms
Essential no
Product endo-1,5-alpha-L-arabinosidase
Function arabinan degradation
Gene expression levels in SubtiExpress: abnA
MW, pI 34 kDa, 8.618
Gene length, protein length 939 bp, 313 aa
Immediate neighbours araA, ysdC
Sequences Protein DNA DNA_with_flanks
Genetic context
AbnA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
AbnA expression.png

















Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

AraR regulon, CcpA regulon

The gene

Basic information

  • Locus tag: BSU28810

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans (according to Swiss-Prot)
  • Protein family: glycosyl hydrolase 43 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

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • repressed in the absence of arabinose (AraR) PubMed
    • subject to carbon catabolite repression (CcpA) PubMed
  • Regulatory mechanism:
  • Additional information: the mRNA is very stable (half-life > 15 min) PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

Teresa Fontes Leal, Isabel de Sá-Nogueira
Purification, characterization and functional analysis of an endo-arabinanase (AbnA) from Bacillus subtilis.
FEMS Microbiol Lett: 2004, 241(1);41-8
[PubMed:15556708] [WorldCat.org] [DOI] (P p)

Maria Paiva Raposo, José Manuel Inácio, Luís Jaime Mota, Isabel de Sá-Nogueira
Transcriptional regulation of genes encoding arabinan-degrading enzymes in Bacillus subtilis.
J Bacteriol: 2004, 186(5);1287-96
[PubMed:14973026] [WorldCat.org] [DOI] (P p)

G Hambraeus, C von Wachenfeldt, L Hederstedt
Genome-wide survey of mRNA half-lives in Bacillus subtilis identifies extremely stable mRNAs.
Mol Genet Genomics: 2003, 269(5);706-14
[PubMed:12884008] [WorldCat.org] [DOI] (P p)