Difference between revisions of "Sandbox"

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* '''Description:''' Carbon catabolite control protein A, involved in glucose regulation of many genes; represses catabolic genes and activates genes involved in excretion of excess carbon <br/><br/>
+
* '''Description:''' UDP-N-acetylglucosamine 1-carboxyvinyltransferase <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
 
|style="background:#ABCDEF;" align="center"|'''Gene name'''
|''ccpA''
+
|''murAA''
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''graR, alsA, amyR''
+
|style="background:#ABCDEF;" align="center"| '''Synonyms''' || ''murA ''
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Essential''' || no
+
|style="background:#ABCDEF;" align="center"| '''Essential''' || yes [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Product''' || transcriptional regulator
+
|style="background:#ABCDEF;" align="center"| '''Product''' || UDP-N-acetylglucosamine 1-carboxyvinyltransferase
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Function''' || mediates carbon catabolite repression (CCR)
+
|style="background:#ABCDEF;" align="center"|'''Function''' || peptidoglycan (cell wall) biosynthesis
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 36,8 kDa, 5.06
+
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 46 kDa, 5.45 
 
|-
 
|-
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length'''  Gene || 1002 bp, 334 amino acids
+
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length'''  Gene || 1308 bp, 436 aa
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[aroA]]'', ''[[motP]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[spoIID]]'', ''[[ywmB]]''
 
|-
 
|-
|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/ccpA_nucleotide.txt    Gene sequence      (+200bp)  ]'''  
+
|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/murAA_nucleotide.txt    Gene sequence      (+200bp)  ]'''  
|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/ccpA_protein.txt Protein sequence]'''
+
|style="background:#FAF8CC;" align="center"|'''[http://subtiwiki.uni-goettingen.de/murAA_protein.txt Protein sequence]'''
 
|-
 
|-
|colspan="2" | '''Genetic context''' <br/> [[Image:ccpA_context.gif]]
+
|colspan="2" | '''Genetic context''' <br/> [[Image:murAA_context.gif]]
 
|-
 
|-
 
|}
 
|}
Line 30: Line 30:
  
 
<br/><br/>
 
<br/><br/>
 
  
 
=The gene=
 
=The gene=
Line 36: Line 35:
 
=== Basic information ===
 
=== Basic information ===
  
* '''Coordinates:''' 3043210 - 3044211
+
* '''Coordinates:'''
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
  
Loss of carbon catabolite repression.  
+
essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
Loss of PTS-dependent sugar transport due to excessive phosphorylation of [[PtsH |HPr]] by [[HprK]].
 
The mutant is unable to grow on a minimal medium with glucose and ammonium as the only sources of carbon and nitrogen, respectively.
 
  
 
=== Database entries ===
 
=== Database entries ===
  
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/ccpA-motPS.html]
+
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/murAA.html]
  
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG10376]
+
* '''SubtiList entry:''' [http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG11955]
  
 
=== Additional information===
 
=== Additional information===
 +
  
 
=The protein=
 
=The protein=
Line 56: Line 54:
 
=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:''' transcriptional regulator of carbon catabolite repression (CCR)
+
* '''Catalyzed reaction/ biological activity:'''  
  
* '''Protein family:''' LacI family
+
* '''Protein family:'''
  
 
* '''Paralogous protein(s):'''
 
* '''Paralogous protein(s):'''
 
=== Genes controlled by CcpA ===
 
 
* '''Activation by CcpA:''' ''[[pta]]'', ''[[ackA]]'', ''[[ilvB]]-[[ilvH]]-[[ilvC]]-[[leuA]]-[[leuB]]-[[leuC]]-[[leuD]]''
 
 
* '''Repression by CcpA:''' ''[[abbA]], [[amyE]]'', ''[[bglP]]-[[bglH]]'', ''[[bglS]]'', ''[[cccA]]'', ''[[citZ]]-[[icd]]-[[mdh]]'', ''[[levD]]-[[levE]]-[[levF]]-[[levG]]-[[sacC]]'', ''[[licB]]-[[licC]]-[[licA]]-[[licH]]'', ''[[phoP]]-[[phoR]]'', ''[[xylA]]-[[xylB]]'', ''[[xynP]]-[[xynB]]''
 
  
 
=== Extended information on the protein ===
 
=== Extended information on the protein ===
Line 73: Line 65:
  
 
* '''Domains:'''  
 
* '''Domains:'''  
** HTH lacI-type Domain (1 – 58)
 
** DNA binding Domain  (6 – 25)
 
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):''' [[PtsH |HPr]]-Ser46-P, Crh-Ser-46-P
+
* '''Cofactor(s):'''
  
* '''Effectors of protein activity:'''glucose-6-phosphate, fructose-1,6-bisphosphate [http://www.ncbi.nlm.nih.gov/pubmed/17376479?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum Pubmed]
+
* '''Effectors of protein activity:'''
  
* '''Interactions:''' CcpA-[[PtsH |HPr]] [http://www.ncbi.nlm.nih.gov/pubmed/15369672?ordinalpos=3&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum PubMed], CcpA-[[Crh]] [http://www.ncbi.nlm.nih.gov/pubmed/16316990?ordinalpos=2&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum PubMed]
+
* '''Interactions:'''
  
 
* '''Localization:'''
 
* '''Localization:'''
Line 88: Line 78:
 
=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' CcpA-Crh-DNA-complex [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=52326 NCBI], complex with P-Ser-[[PtsH |HPr]] and sulphate ions [http://www.ncbi.nlm.nih.gov/Structure/mmdb/mmdbsrv.cgi?Dopt=s&uid=39857 NCBI]
+
* '''Structure:'''
  
* '''Swiss prot entry:''' [http://www.expasy.ch/cgi-bin/sprot-search-ac?P25144]
+
* '''Swiss prot entry:'''
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU29740]
+
* '''KEGG entry:'''
 +
 
 +
* '''E.C. number:'''
  
 
=== Additional information===
 
=== Additional information===
 +
 +
MurAA is subject to [[ClpC]]-[[ClpP]]-dependent degradation  [http://www.ncbi.nlm.nih.gov/sites/entrez/14763982 PubMed]
  
 
=Expression and regulation=
 
=Expression and regulation=
  
* '''Operon:''' ''[[ccpA]] [[motP]] [[motS]]'' [http://www.ncbi.nlm.nih.gov/sites/entrez/16547058 PubMed]
+
* '''Operon:'''  
  
 
* '''Sigma factor:'''  
 
* '''Sigma factor:'''  
  
* '''Regulation:''' constitutively  expressed [http://www.ncbi.nlm.nih.gov/sites/entrez/18757537 PubMed]
+
* '''Regulation:'''  
 +
 
 +
* '''Regulatory mechanism:'''
  
* '''Additional information:''' there are about 3.000 molecules of CcpA per cell [http://www.ncbi.nlm.nih.gov/sites/entrez/8000527 PubMed]
+
* '''Additional information:'''  
  
 
=Biological materials =
 
=Biological materials =
  
* '''Mutant:''' QB5407 (spc), GP302 (erm), GP300 (an in frame deletion of ccpA), available in [[Stülke]] lab
+
* '''Mutant:'''
  
* '''Expression vector:''' pGP643 (in [[pGP380]], for SPINE, expression in Bacillus subtilis)
+
* '''Expression vector:'''
+
       
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''
  
 
* '''GFP fusion:'''
 
* '''GFP fusion:'''
  
* '''Antibody:''' available in [[Hillen]] and [[Stülke]] labs
+
* '''two-hybrid system:'''
 +
 
 +
* '''Antibody:'''
  
 
=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
 
[[Wolfgang Hillen]], Erlangen University, Germany [http://www.biologie.uni-erlangen.de/mibi/index2.html Homepage]
 
 
[[Richard Brennan]], Houston, Texas, USA [http://www.mdanderson.org/departments/biochem/display.cfm?id=556ef368-6c81-4043-b74f350d41dd06cb&method=displayfull&pn=a8427ebd-d0ff-11d4-80fd00508b603a14 Homepage]
 
 
[[Milton H. Saier]], University of California at San Diego, USA [http://biology.ucsd.edu/faculty/saier.html Homepage]
 
 
[[Yasutaro Fujita]], University of Fukuyama, Japan
 
 
[[Stülke|Jörg Stülke]], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
 
  
 
=Your additional remarks=
 
=Your additional remarks=
Line 134: Line 122:
 
=References=
 
=References=
  
'''Reviews'''
+
# Kock H, Gerth U, Hecker M. (2004) MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis. Mol Microbiol, 51:1087-1102. [http://www.ncbi.nlm.nih.gov/sites/entrez/14763982 PubMed]
 
+
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
# Henkin, T. M. (1996) The role of the CcpA transcriptional regulator in carbon metabolism in Bacillus subtilis. FEMS Microbiol Lett 135: 9-15. [http://www.ncbi.nlm.nih.gov/sites/entrez/8598282 PubMed]
 
# Warner, J. B. & Lolkema, J. S. CcpA-dependent carbon catabolite repression in bacteria. Microbiol. Mol. Biol. Rev. 67, 475-490 (2003). [http://www.ncbi.nlm.nih.gov/sites/entrez/14665673 PubMed]
 
 
 
'''General and physiological studies'''
 
 
 
# Henkin, T. M., Grundy, F. J., Nicholson, W. L. and Chambliss, G. H. (1991) Catabolite repression of -amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacI and galR repressors. Mol. Microbiol. 5, 575-584. [http://www.ncbi.nlm.nih.gov/sites/entrez/1904524 PubMed]
 
# Faires, N., Tobisch, S., Bachem, S., Martin-Verstraete, I., Hecker, M., & Stülke, J. (1999) The catabolite control protein CcpA controls ammonium assimilation in Bacillus subtilis. J. Mol. Microbiol. Biotechnol. 1: 141-148. [http://www.ncbi.nlm.nih.gov/sites/entrez/10941796 PubMed]
 
# Ludwig, H., Rebhan, N., Blencke, H.-M., Merzbacher, M. & Stülke, J. (2002) Control of the glycolytic gapA operon by the catabolite control protein A in Bacillus subtilis: a novel mechanism of CcpA-mediated regulation. Mol. Microbiol. 45: 543-553. [http://www.ncbi.nlm.nih.gov/sites/entrez/12123463 PubMed]
 
# Miwa, Y., M. Saikawa, and Y. Fujita. 1994. Possible function and some properties of the CcpA protein of Bacillus subtilis. Microbiology 140:2567-2575. [http://www.ncbi.nlm.nih.gov/sites/entrez/8000527 PubMed]
 
# Singh, K. D., Schmalisch, M. H., Stülke, J. & Görke, B. (2008) Carbon catabolite repression in Bacillus subtilis: A quantitative analysis of repression exerted by different carbon sources. J. Bacteriol. 190: 7275-7284. [http://www.ncbi.nlm.nih.gov/sites/entrez/18757537 PubMed]
 
# Terahara et al. (2006) An intergenic stem-loop mutation in the Bacillus subtilis ccpA-motPS operon increases motPS transcription and the MotPS contribution to motility ''J Bacteriol.'' '''188:''' 2701-2705. [http://www.ncbi.nlm.nih.gov/sites/entrez/16547058 PubMed]
 
# Wacker, I., Ludwig, H., Reif, I., Blencke, H.-M., Detsch, C. & Stülke, J. (2003) The regulatory link between carbon and nitrogen metabolism in Bacillus subtilis: regulation of the gltAB operon by the catabolite control protein CcpA. Microbiology 149:  3001-3009. [http://www.ncbi.nlm.nih.gov/sites/entrez/14523131 PubMed]
 
 
 
'''Global analyses (proteome, transcriptome)'''
 
 
 
# Blencke, H.-M., Homuth, G., Ludwig, H., Mäder, U., Hecker, M. & Stülke, J. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab. Engn. 5: 133-149. [http://www.ncbi.nlm.nih.gov/sites/entrez/12850135 PubMed]
 
# Moreno MS, Schneider BL, Maile RR, Weyler W, Saier Jr MH: Catabolite repression mediated by CcpA protein in Bacillus subtilis: novel modes of regulation revealed by whole-genome analysis. Mol Microbiol 2001, 39:1366-1381. [http://www.ncbi.nlm.nih.gov/sites/entrez/11251851 PubMed]
 
# Tobisch, S., Zühlke, D., Bernhardt, J., Stülke, J. & Hecker, M. (1999) Role of CcpA in regulation of the central pathways of carbon catabolism in Bacillus subtilis. J. Bacteriol. 181: 6996-7004. [http://www.ncbi.nlm.nih.gov/sites/entrez/10559165 PubMed]
 
# Yoshida, K.-I., Kobayashi, K., Miwa, Y., Kang, C.-M., Matsunaga, M., Yamaguchi, H., Tojo, S., Yamamoto, M., Nishi, R., Ogasawara, N., Nakayama, T. & Fujita, Y. (2001). Combined transcriptome and proteome analysis as a powerful approach to study genes under glucose repression in Bacillus subtilis. Nucl Acids Res 29, 6683-6692. [http://www.ncbi.nlm.nih.gov/sites/entrez/11160890 PubMed]
 
# Lulko, A. T., G. Buist, J. Kok, and O. P. Kuipers. 2007. Transcriptome analysis of temporal regulation of carbon metabolism by CcpA in ''Bacillus subtilis'' reveals additional target genes. J. Mol. Microbiol. Biotechnol. 12:82-95. [http://www.ncbi.nlm.nih.gov/sites/entrez/17183215 PubMed]
 
 
 
'''Repression of target genes by CcpA'''
 
 
 
# Belitsky BR, Sonenshein, AL: CcpA-dependent regulation of Bacillus subtilis glutamate dehydrogenase gene expression. J Bacteriol 2004, 186:3392-3398. [http://www.ncbi.nlm.nih.gov/sites/entrez/15150224 PubMed]
 
# Choi SK, Saier MH Jr: Regulation of sigL expression by the catabolite control protein CcpA involves a roadblock mechanism in Bacillus subtilis: potential connection between carbon and nitrogen metabolism. J Bacteriol 2005, 187:6856-6861. [http://www.ncbi.nlm.nih.gov/sites/entrez/16166551 PubMed]
 
# Darbon, E., Servant, P., Poncet, S., and Deutscher, J. (2002). Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P~GlpK dephosphorylation control Bacillus subtilis glpFK expression. Mol. Microbiol. 43, 1039-1052. [http://www.ncbi.nlm.nih.gov/sites/entrez/11929549 PubMed]
 
# Grundy, F. J., Turinski, A. J., and Henkin, T. M. (1994). Catabolite regulation of Bacillus subtilis acetate and acetoin utilization genes by CcpA. J. Bacteriol. 176, 4527-4533. [http://www.ncbi.nlm.nih.gov/sites/entrez/7913927 PubMed]
 
# Inacio, J. M. & de Sá-Nogueira, I. trans-Acting factors and cis-elements involved in glucose repression of arabinan degradation in Bacillus subtilis. J. Bacteriol. 189, 8371-8376 (2007). [http://www.ncbi.nlm.nih.gov/sites/entrez/17827291 PubMed]
 
# Kim HJ, Jourlin-Castelli C, Kim SI, Sonenshein AL (2002) Regulation of the Bacillus subtilis ccpC gene by CcpA and CcpC. Mol Microbiol 43:399-410 [http://www.ncbi.nlm.nih.gov/sites/entrez/11985717 PubMed]
 
# Kim HJ, Roux A, Sonenshein AL (2002) Direct and indirect roles of CcpA in regulation of Bacillus subtilis Krebs cycle genes. Mol Microbiol 45:179-190 [http://www.ncbi.nlm.nih.gov/sites/entrez/12100558 PubMed]
 
# Martin-Verstraete, I., Stülke, J., Klier, A. & Rapoport, G. (1995) Two different mechanisms mediate catabolite repression of the Bacillus subtilis levanase operon. J. Bacteriol. 177: 6919-6927. [http://www.ncbi.nlm.nih.gov/sites/entrez/7592486 PubMed]
 
 
 
'''Positive regulation of gene expression by CcpA'''
 
 
 
# Grundy FJ, Waters DA, Allen SH, Henkin TM (1993) Regulation of the Bacillus subtilis acetate kinase gene by CcpA. J Bacteriol 175:7348-7355 [http://www.ncbi.nlm.nih.gov/sites/entrez/8226682 PubMed]
 
# Ludwig, H., Meinken, C., Matin, A. & Stülke, J. (2002) Insufficient expression of the ilv-leu operon encoding enzymes of branched-chain amino acids biosynthesis limits growth of a Bacillus subtilis ccpA mutant. J. Bacteriol. 184: 5174-5178. [http://www.ncbi.nlm.nih.gov/sites/entrez/12193635 PubMed]
 
# Presecan-Siedel, E., Galinier, A., Longin, R., Deutscher, J., Danchin, A., Glaser, P. and Martin-Verstraete, I. (1999) The catabolite regulation of the pta gene as part of carbon flow pathways in Bacillus subtilis. J. Bacteriol. 181, 6889-6897. [http://www.ncbi.nlm.nih.gov/sites/entrez/10559153 PubMed]
 
# Shivers, R. P., and Sonenshein, A. L. (2005) Bacillus subtilis ilvB operon: an intersection of global regulons. Mol Microbiol 56: 1549-1559. [http://www.ncbi.nlm.nih.gov/sites/entrez/15916605 PubMed]
 
# Turinsky, A. J., Grundy, F. J., Kim, J. H., Chambliss, G. H., and Henkin, T. M. 1998. Transcriptional activation of the Bacillus subtilis ackA gene requires sequences upstream of the promoter. J. Bacteriol. 180: 5961-5967. [http://www.ncbi.nlm.nih.gov/sites/entrez/9811655 PubMed]
 
# Turinsky, A. J., Moir-Blais, T. R., Grundy, F. J., and Henkin, T. M. 2000. Bacillus subtilis ccpA gene mutants specifically defective in activation of acetoin synthesis. J. Bacteriol. 182:5611-5614. [http://www.ncbi.nlm.nih.gov/sites/entrez/10986270 PubMed]
 
 
 
'''Control of CcpA activity'''
 
 
 
# Deutscher, J., Küster, E., Bergstedt, U., Charrier, V., and Hillen, W. 1995. Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in Gram-positive bacteria. Mol. Microbiol. 15: 1049-1053. [http://www.ncbi.nlm.nih.gov/sites/entrez/7623661 PubMed]
 
# Galinier A, Deutscher J, Martin-Verstraete I: Phosphorylation of either Crh or HPr mediates binding of CcpA to the Bacillus subtilis xyn cre and catabolite repression of the xyn operon. J Mol Biol 1999, 286:307-314. [http://www.ncbi.nlm.nih.gov/sites/entrez/9973552 PubMed]
 
# Jones, B. E., Dossonnet, V., Küster, E., Hillen, W., Deutscher, J. & Klevit, R. E. (1997). Binding of the catabolite repressor protein CcpA to its DNA target is regulated by phosphorylation of its corepressor HPr. J Biol Chem 272, 26530-26535. [http://www.ncbi.nlm.nih.gov/sites/entrez/9334231 PubMed]
 
# Aung-Hilbrich LM, Seidel G, Wagner A, Hillen W (2002) Quantification of the influence of HPrSer46P on CcpA-cre interaction. J Mol Biol 319:77-85. [http://www.ncbi.nlm.nih.gov/sites/entrez/12051938 PubMed]
 
# Kim JH, Voskuil MI, Chambliss GH (1998) NADP, corepressor for the ''Bacillus subtilis'' catabolite control protein CcpA. Proc Natl Acad Sci USA 95:9590-9595. [http://www.ncbi.nlm.nih.gov/sites/entrez/9689125 PubMed]
 
 
 
'''CcpA-DNA interaction'''
 
 
 
# Fujita, Y., Miwa, Y., Galinier, A. and Deutscher, J. (1995) Specific recognition of the ''Bacillus subtilis gnt cis''-acting catabolite-responsive element by a protein complex formed between CcpA and seryl-phosphorylated HPr. Mol. Microbiol. 17, 953-960. [http://www.ncbi.nlm.nih.gov/sites/entrez/8596444 PubMed]
 
# Miwa, Y., Nakata, A., Ogiwara, A., Yamamota, M., and Fujita, Y. 2000. Evaluation and characterization of catabolite-responsive elements (cre) of ''Bacillus subtilis''. Nucl. Acids Res. 28: 1206-1210. [http://www.ncbi.nlm.nih.gov/sites/entrez/10666464 PubMed]
 
# Seidel G, Diel M, Fuchsbauer N, Hillen W: Quantitative interdependence of coeffectors, CcpA and cre in carbon catabolite regulation of ''Bacillus subtilis''. FEBS J 2005, 272:2566-2577. [http://www.ncbi.nlm.nih.gov/sites/entrez/15885105 PubMed]
 
# Kim JH, Guvener ZT, Cho JY, Chung KC, Chambliss GH (1995) Specificity of DNA binding activity of the ''Bacillus subtilis'' catabolite control protein CcpA. J Bacteriol 177: 5129-5134. [http://www.ncbi.nlm.nih.gov/sites/entrez/7665492 PubMed]
 
# Kim JH, Chambliss GH (1997) Contacts between ''Bacillus subtilis'' catabolite regulatory protein CcpA and ''amyO'' target site. Nucl Acids Res 25: 3490-3496. [http://www.ncbi.nlm.nih.gov/sites/entrez/9254709 PubMed]
 
 
 
 
 
 
 
'''Functional analysis of CcpA'''
 
 
 
# Küster, E., Hilbich, T., Dahl, M. and Hillen, W. (1999) Mutations in catabolite control protein CcpA separating growth effects from catabolite repression. J. Bacteriol. 181, 4125-4128. [http://www.ncbi.nlm.nih.gov/sites/entrez/10383986 PubMed]
 
# Küster-Schöck, E., Wagner, A., Völker, U., and Hillen, W. (1999) Mutations in catabolite control protein CcpA showing glucose-independent regulation in ''Bacillus megaterium''. J Bacteriol 181: 7634-7638. [http://www.ncbi.nlm.nih.gov/sites/entrez/10601226 PubMed]
 
# Ludwig, H. & Stülke, J. (2001) The Bacillus subtilis catabolite control protein CcpA exerts all its regulatory functions by DNA binding. FEMS Microbiol. Lett. 203: 125-129. [http://www.ncbi.nlm.nih.gov/sites/entrez/11557150 PubMed]
 
# Kraus A, Hillen W. 1997. Analysis of ccpA mutations defective in carbon catabolite repression in Bacillus megaterium. FEMS Microbiol. Lett. 153:221-226. [http://www.ncbi.nlm.nih.gov/sites/entrez/9252590 PubMed]
 
# Kraus A, Küster E, Wagner A, Hoffmann K, Hillen W. 1998. Identification of a corepressor binding site in catabolite control protein CcpA. Mol. Microbiol. 30:955-963. [http://www.ncbi.nlm.nih.gov/sites/entrez/9988473 PubMed]
 
 
 
 
 
'''Structural analyses'''
 
 
 
# Schumacher, M. A. et al. Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P. Cell 118, 731-741 (2004). [http://www.ncbi.nlm.nih.gov/sites/entrez/15369672 PubMed]
 
# Schumacher, M. A., Seidel, G., Hillen, W. & Brennan, R. G. Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation. J. Biol. Chem. 281, 6793-6800 (2006). [http://www.ncbi.nlm.nih.gov/sites/entrez/16316990 PubMed]
 
# Schumacher, M. A., Seidel, G., Hillen, W. & Brennan, R. G. Structural mechanism for the fine-tuning of CcpA function by the small molecule effectors glucose 6-phosphate and fructose 1,6-bisphosphate. J. Mol. Biol. 368, 1042-1050 (2007). [http://www.ncbi.nlm.nih.gov/sites/entrez/17376479 PubMed]
 

Revision as of 10:01, 18 March 2009

  • Description: UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Gene name murAA
Synonyms murA
Essential yes PubMed
Product UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Function peptidoglycan (cell wall) biosynthesis
MW, pI 46 kDa, 5.45
Gene length, protein length Gene 1308 bp, 436 aa
Immediate neighbours spoIID, ywmB
Gene sequence (+200bp) Protein sequence
Genetic context
MurAA context.gif



The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • Structure:
  • Swiss prot entry:
  • KEGG entry:
  • E.C. number:

Additional information

MurAA is subject to ClpC-ClpP-dependent degradation PubMed

Expression and regulation

  • Operon:
  • Sigma factor:
  • 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

  1. Kock H, Gerth U, Hecker M. (2004) MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis. Mol Microbiol, 51:1087-1102. PubMed
  2. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed