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| * '''Description:''' protein acetylase for the control of AcsA activity <br/><br/>
| | {{#bank: AcuA}} |
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| {| align="right" border="1" cellpadding="2"
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| |style="background:#ABCDEF;" align="center"|'''Gene name'''
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| |''acuA''
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| |-
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| |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
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| |style="background:#ABCDEF;" align="center"| '''Essential''' || no
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| |style="background:#ABCDEF;" align="center"| '''Product''' || Gcn5-related N-acetyltransferase
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| |style="background:#ABCDEF;" align="center"|'''Function''' || control of AcsA activity
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| |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 24 kDa, 5.028
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| |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 630 bp, 210 aa
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| |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[acsA]]'', ''[[acuB]]''
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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+[EMBLCDS:CAB14947]+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
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| |colspan="2" | '''Genetic context''' <br/> [[Image:acuA_context.gif]]
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| <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
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| |}
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| __TOC__
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| <br/><br/>
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| =The gene=
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| === Basic information ===
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| * '''Coordinates:'''
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| ===Phenotypes of a mutant ===
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| === Database entries ===
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| * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/acuABC.html]
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| * '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10369]
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| === Additional information===
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| =The protein=
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| === Basic information/ Evolution ===
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| * '''Catalyzed reaction/ biological activity:''' acetylates (and thereby inactivates) [[AcsA]] on Lys-549 [http://www.ncbi.nlm.nih.gov/sites/entrez/18487328 PubMed] [http://www.ncbi.nlm.nih.gov/sites/entrez/19136592 PubMed]
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| * '''Protein family:''' acetyltransferase family (according to Swiss-Prot) Gcn5-relatedN-acetyltransferase [http://www.ncbi.nlm.nih.gov/sites/entrez/18487328 PubMed]
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| * '''Paralogous protein(s):'''
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| === Extended information on the protein ===
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| * '''Kinetic information:'''
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| * '''Domains:'''
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| * '''Modification:'''
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| * '''Cofactor(s):'''
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| * '''Effectors of protein activity:'''
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| * '''Interactions:'''
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| * '''Localization:'''
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| === Database entries ===
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| * '''Structure:'''
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| * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P39065 P39065]
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| * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU29690 BSU29690]
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| * '''E.C. number:'''
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| === Additional information===
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| =Expression and regulation=
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| * '''Operon:'''
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| * '''[[Sigma factor]]:'''
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| * '''Regulation:''' repressed by glucose (3.4-fold) ([[CcpA]]) [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
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| * '''Regulatory mechanism:''' [[CcpA]]: transcription repression
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| * '''Additional information:'''
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| =Biological materials =
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| * '''Mutant:'''
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| * '''Expression vector:'''
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| * '''lacZ fusion:'''
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| * '''GFP fusion:'''
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| * '''two-hybrid system:'''
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| * '''Antibody:'''
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| =Labs working on this gene/protein=
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| =Your additional remarks=
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| =References=
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| # Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in ''Bacillus subtilis'': regulation of the central metabolic pathways. ''Metab Eng.'' '''5:''' 133-149 [http://www.ncbi.nlm.nih.gov/pubmed/12850135 PubMed]
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| # Gardner JG, Escalante-Semerena JC (2008) Biochemical and mutational analyses of AcuA, the acetyltransferase enzyme that controls the activity of the acetyl coenzyme a synthetase (AcsA) in ''Bacillus subtilis''. ''J. Bacteriol.'' '''190:''' 5132-5136. [http://www.ncbi.nlm.nih.gov/sites/entrez/18487328 PubMed]
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| # Gardner JG, Escalante-Semerena JC (2009) In ''Bacillus subtilis'', the sirtuin protein deacetylase, encoded by the ''srtN'' gene (formerly ''yhdZ''), and functions encoded by the ''acuABC'' genes control the activity of acetyl coenzyme A synthetase. ''J. Bacteriol.'' '''191:''' 1749-1755. [http://www.ncbi.nlm.nih.gov/sites/entrez/19136592 PubMed]
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| # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
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