Difference between revisions of "PrkC"
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===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
* unable to germinate in response to muropeptides {{PubMed|18984160}} | * unable to germinate in response to muropeptides {{PubMed|18984160}} | ||
| + | * reduced growth at high salt {{PubMed|25845974}} | ||
=== Database entries === | === Database entries === | ||
| Line 93: | Line 94: | ||
* '''[[Cofactors]]:''' | * '''[[Cofactors]]:''' | ||
| − | * '''Effectors of protein activity:''' activated by muropeptides {{PubMed|18984160}} | + | * '''Effectors of protein activity:''' |
| + | ** activated by muropeptides {{PubMed|18984160}} | ||
| + | ** [[GpsB]], [[DivIVA]], and [[EzrA]] are required for stimulation of [[PrkC]] activity {{PubMed|25845974}} | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
** [[AbrB]]-[[PrkC]] {{PubMed|24731262}} | ** [[AbrB]]-[[PrkC]] {{PubMed|24731262}} | ||
** [[YvcK]]-[[PrkC]] {{PubMed|25012659}} | ** [[YvcK]]-[[PrkC]] {{PubMed|25012659}} | ||
| + | ** [[GpsB]]-[[PrkC]] {{PubMed|25845974}} | ||
| − | * '''[[Localization]]:''' inner spore membrane {{PubMed|18984160}} | + | * '''[[Localization]]:''' |
| + | ** inner spore membrane {{PubMed|18984160}} | ||
| + | ** membrane [http://www.ncbi.nlm.nih.gov/sites/entrez/12406230 PubMed] | ||
| + | ** division septum {{PubMed|25845974}} | ||
=== Database entries === | === Database entries === | ||
Revision as of 15:53, 10 April 2015
- Description: protein kinase C, induce germination of spores in response to DAP-type, and not to Lys-type cell wall muropeptides
| Gene name | prkC |
| Synonyms | yloP |
| Essential | no |
| Product | protein kinase |
| Function | germination in response to muropeptides |
| Gene expression levels in SubtiExpress: prkC | |
| Interactions involving this protein in SubtInteract: PrkC | |
| Metabolic function and regulation of this protein in SubtiPathways: prkC | |
| MW, pI | 71 kDa, 4.833 |
| Gene length, protein length | 1944 bp, 648 aa |
| Immediate neighbours | prpC, cpgA |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
protein modification, germination, membrane proteins, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15770
Phenotypes of a mutant
Database entries
- BsubCyc: BSU15770
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + a protein = ADP + a phosphoprotein (according to Swiss-Prot)
- Protein family: protein kinase domain (according to Swiss-Prot)
- Paralogous protein(s):
Proteins phosphorylated by PrkC
CpgA, EF-Tu, YezB PubMed, EF-G PubMed, YwjH, GlnA, Icd, AlsD, HPr PubMed, YkwC PubMed, YvcK PubMed, GpsB PubMed
Extended information on the protein
- Kinetic information:
- Domains:
- contains three C-terminal PASTA domains (aa 356-424, 425-492, 493-559) (binds muropeptides) PubMed
- Modification: phosphorylation on Thr-290 PubMed, autophosphorylation on multiple threonine residues PubMed
- Effectors of protein activity:
Database entries
- BsubCyc: BSU15770
- Structure:
- UniProt: O34507
- KEGG entry: [2]
- E.C. number: 2.7.11.1
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP576 (spc), OMG302 (aphA3), available in Stülke lab
- Expression vector:
- for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP832, available in Stülke lab
- for expression/ purification of the kinase domain from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP849, available in Stülke lab
- for expression, purification in E. coli with N-terminal His-tag, in pWH844: pGP1001, available in Stülke lab
- for expression, purification in E. coli with N-terminal Strep-tag, in pGP172: pGP825, available in Stülke lab
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Phosphorylation of PrkC
Targets of PrkC-dependent phosphorylation
Phsiological role of PrkC
Expression of PrkC
Structure/ biochemistry of PrkC
Rita Berisio, Flavia Squeglia, Alessia Ruggiero, Luigi Petraccone, Marco Ignazio Stellato, Pompea Del Vecchio
Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies.
Biochim Biophys Acta: 2015, 1854(5);402-9
[PubMed:25668224]
[WorldCat.org]
[DOI]
(P p)
Tristan Wagner, Matthieu Alexandre, Rosario Duran, Nathalie Barilone, Annemarie Wehenkel, Pedro M Alzari, Marco Bellinzoni
The crystal structure of the catalytic domain of the ser/thr kinase PknA from M. tuberculosis shows an Src-like autoinhibited conformation.
Proteins: 2015, 83(5);982-8
[PubMed:25586004]
[WorldCat.org]
[DOI]
(I p)
Gunjan Arora, Andaleeb Sajid, Mary Diana Arulanandh, Richa Misra, Anshika Singhal, Santosh Kumar, Lalit K Singh, Abid R Mattoo, Rishi Raj, Souvik Maiti, Sharmila Basu-Modak, Yogendra Singh
Zinc regulates the activity of kinase-phosphatase pair (BasPrkC/BasPrpC) in Bacillus anthracis.
Biometals: 2013, 26(5);715-30
[PubMed:23793375]
[WorldCat.org]
[DOI]
(I p)
Flavia Squeglia, Roberta Marchetti, Alessia Ruggiero, Rosa Lanzetta, Daniela Marasco, Jonathan Dworkin, Maxim Petoukhov, Antonio Molinaro, Rita Berisio, Alba Silipo
Chemical basis of peptidoglycan discrimination by PrkC, a key kinase involved in bacterial resuscitation from dormancy.
J Am Chem Soc: 2011, 133(51);20676-9
[PubMed:22111897]
[WorldCat.org]
[DOI]
(I p)
Alessia Ruggiero, Flavia Squeglia, Daniela Marasco, Roberta Marchetti, Antonio Molinaro, Rita Berisio
X-ray structural studies of the entire extracellular region of the serine/threonine kinase PrkC from Staphylococcus aureus.
Biochem J: 2011, 435(1);33-41
[PubMed:21208192]
[WorldCat.org]
[DOI]
(I p)
