prkC

prkC
168

protein kinase C, fine-tuning of cell growth rates in response to Lipid II in different nutrient conditions, induces Germination of spores in response to DAP-type, and not to Lys-type cell wall muropeptides, stimulates WalR activity

Locus
BSU_15770
Molecular weight
71.69 kDa
Isoelectric point
4.83
Protein length
Gene length
Function
regulation of growth and germination in response to muropeptides and Lipid II
Product
protein kinase
Essential
no
E.C.
2.7.11.1
Synonyms
prkC, yloP

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG2815 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
1,651,142  1,653,088
Phenotypes of a mutant
unable to germinate in response to muropeptides PubMed
reduced growth at high salt PubMed
The protein
Catalyzed reaction/ biological activity
phosphorylation of WalR on Thr-101 to stimulate its activity PubMed
phosphorylates PrkA on Thr-217 PubMed
phosphorylation of RodZ in response to lipid II abundance PubMed
Protein family
protein kinase superfamily (according to UniProt)
Ser/Thr protein kinase family (according to UniProt)
contains three C-terminal PASTA domains (aa 356-424, 425-492, 493-559) (binds muropeptides) PubMed
Protein kinase domain (aa 11-271) (according to UniProt)
Structure
4EQM (PDB) (intracellular domain of the Staphylococcus aureus enzyme, 51% identity) PubMed
3PY9 (PDB) (entire extra-cellular region of PrkC from Staphylococcus aureusPubMed
4X3F (PDB) (intracellular domain of the Mycobacterium tuberculosis enzyme, 36% identity, 68% similarity) PubMed
Modification
phosphorylation on Thr-290 PubMed, autophosphorylation on multiple threonine residues PubMed
Effectors of protein activity
activated by muropeptides PubMed
lipid II PubMed
GpsB, DivIVA, and EzrA are required for stimulation of PrkC activity PubMed
inner spore membrane PubMed
membrane PubMed
division septum PubMed
Expression and Regulation
Operons
Description
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prpCyloS

2025-03-17 16:32:40

Jstuelk

128

f45e3810755c3fba238243b21c1c17e072c8fe47

14D2827FA6BD60210DFADC1BB1FFF0C98DC768FA

Biological materials
Mutant
MGNA-B134 (yloP::erm), available at the NBRP B. subtilis, Japan
GP576 (spc), OMG302 (aphA3), available in Jörg Stülke's lab
1A820 ( prkC::erm), PubMed, available at BGSC
1A963 (no resistance), PubMed, available at BGSC
1A964 (no resistance), PubMed, available at BGSC
BKE15770 (prkC::erm  trpC2) available at BGSCPubMed, upstream reverse: _UP1_GATTAGCACTGATCTTCACC,  downstream forward: _UP4_GATGAATAACAAGGAGGGAA
BKK15770 (prkC::kan  trpC2) available at BGSCPubMed, upstream reverse: _UP1_GATTAGCACTGATCTTCACC,  downstream forward: _UP4_GATGAATAACAAGGAGGGAA
Expression vectors
for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP832, available in Jörg Stülke's lab
for expression/ purification of the kinase domain from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP849, available in Jörg Stülke's lab
for expression, purification in E. coli with N-terminal His-tag, in pWH844: pGP1001,  available in Jörg Stülke's lab
for expression, purification in E. coli with N-terminal Strep-tag, in pGP172: pGP825,  available in Jörg Stülke's lab, PubMed
LacZ fusion
pGP829 (in pAC7), available in Jörg Stülke's lab
References
Reviews
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Phosphorylation of PrkC
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Phsiological role of PrkC
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Structure/ biochemistry of PrkC
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Expression/ localization of PrkC
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Targets of PrkC-dependent phosphorylation
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23FF4A00C36EC1B7297F51A9EF3579B41F0B7EBA

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Time of last update: 2025-04-03 23:57:45

Author of last update: Jstuelk