⊟Summary[edit | edit source]
- pan ID?: SAUPAN005508000
- symbol?: dacA
- synonym:
- description?: ABC transporter permease
- ABC transporter permease
- diadenylate cyclase CdaA
- hypothetical protein with TIGR00159 domain
- TIGR00159 family protein
- ABC transporter, permease protein YbbP clustered with maltose/maltodextrin transporter / Tlr1762 protein
- checkpoint controller nucleotide-binding protein
- disA bacterial checkpoint controller nucleotide-binding family protein
- membrane protein
- membrane spanning protein
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 5673094..5673729
- synteny block?: BlockID0042900
- occurrence?: in 100% of 34 strains
dacA (cdaA) : diadenylate cyclase [1]
• A crystal structure is available : 6GYW
Bacteria need to carefully balance their intracellular osmolyte concentration with peptidoglycan synthesis to ensure the cell's structural integrity can tolerate the cell's turgor pressure. Staphylococci do this using the second messenger nucleotide cyclic-di-AMP which positively regulates osmolyte uptake. This is coupled with cell wall synthesis through the dacA-cdaR-glmM operon. DacA is a diadenylate cyclase which generates the nucleotide second messenger signal cyclic-di-AMP, a positive regulator of potassium and compatible solute influx transporters. CdaR is a positive regulator of the three-gene operon while GlmM encodes phosphoglucosamine mutase that generates the peptidoglycan precursor glucosamine-1-phosphate. To prevent runaway amplification of cyclic-di-AMP levels, GlmM binds and inhibits DacA. Therefore, when cell wall integrity is insufficient, GlmM is stimulated and reduces cyclic-di-AMP-mediated turgor pressure until the cell wall can accommodate the increased intracellular pressure.
⊟Orthologs[edit | edit source]
⊟Genome Viewer[edit | edit source]
| COL | |
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL MDFSNFFQNLSTLKIVTSILDLLIVWYVLYLLITVFKGTKAIQLLKGILVIVIGQQISMI
N315 MDFSNFFQNLSTLKIVTSILDLLIVWYVLYLLITVFKGTKAIQLLKGILVIVIGQQISMI
NCTC8325 MDFSNFFQNLSTLKIVTSILDLLIVWYVLYLLITVFKGTKAIQLLKGILVIVIGQQISMI
Newman MDFSNFFQNLSTLKIVTSILDLLIVWYVLYLLITVFKGTKAIQLLKGILVIVIGQQISMI
USA300_FPR3757 MDFSNFFQNLSTLKIVTSILDLLIVWYVLYLLITVFKGTKAIQLLKGILVIVIGQQISMI
************************************************************
COL LNLTATSKLFDIVIQWGVLALIVIFQPEIRRALEQLGRGSFLKRYTSNTYSKDEEKLIQS
N315 LNLTATSKLFDIVIQWGVLALIVIFQPEIRRALEQLGRGSFLKRYTSNTYSKDEEKLIQS
NCTC8325 LNLTATSKLFDIVIQWGVLALIVIFQPEIRRALEQLGRGSFLKRYTSNTYSKDEEKLIQS
Newman LNLTATSKLFDIVIQWGVLALIVIFQPEIRRALEQLGRGSFLKRYTSNTYSKDEEKLIQS
USA300_FPR3757 LNLTATSKLFDIVIQWGVLALIVIFQPEIRRALEQLGRGSFLKRYTSNTYSKDEEKLIQS
************************************************************
COL VSKAVQYMAKRRIGALIVFEKETGLQDYIETGIAMDSNISQELLINVFIPNTPLHDGAMI
N315 VSKAVQYMAKRRIGALIVFEKETGLQDYIETGIAMDSNISQELLINVFIPNTPLHDGAMI
NCTC8325 VSKAVQYMAKRRIGALIVFEKETGLQDYIETGIAMDSNISQELLINVFIPNTPLHDGAMI
Newman VSKAVQYMAKRRIGALIVFEKETGLQDYIETGIAMDSNISQELLINVFIPNTPLHDGAMI
USA300_FPR3757 VSKAVQYMAKRRIGALIVFEKETGLQDYIETGIAMDSNISQELLINVFIPNTPLHDGAMI
************************************************************
COL IQGTKIAAAASYLPLSDSPKISKSLGTRHRAAVGISEVSDAFTVIVSEETGDISVTFDGK
N315 IQGTKIAAAASYLPLSDSPKISKSLGTRHRAAVGISEVSDAFTVIVSEETGDISVTFDGK
NCTC8325 IQGTKIAAAASYLPLSDSPKISKSLGTRHRAAVGISEVSDAFTVIVSEETGDISVTFDGK
Newman IQGTKIAAAASYLPLSDSPKISKSLGTRHRAAVGISEVSDAFTVIVSEETGDISVTFDGK
USA300_FPR3757 IQGTKIAAAASYLPLSDSPKISKSLGTRHRAAVGISEVSDAFTVIVSEETGDISVTFDGK
************************************************************
COL LRRDISNEIFEELLAEHWFGTRFQKKGVK
N315 LRRDISNEIFEELLAEHWFGTRFQKKGVK
NCTC8325 LRRDISNEIFEELLAEHWFGTRFQKKGVK
Newman LRRDISNEIFEELLAEHWFGTRFQKKGVK
USA300_FPR3757 LRRDISNEIFEELLAEHWFGTRFQKKGVK
*****************************
- ↑ Tommaso Tosi, Fumiya Hoshiga, Charlotte Millership, Rahul Singh, Charles Eldrid, Delphine Patin, Dominique Mengin-Lecreulx, Konstantinos Thalassinos, Paul Freemont, Angelika Gründling
Inhibition of the Staphylococcus aureus c-di-AMP cyclase DacA by direct interaction with the phosphoglucosamine mutase GlmM.
PLoS Pathog: 2019, 15(1);e1007537
[PubMed:30668586] [WorldCat.org] [DOI] (I e)