Literature summary for 2.3.2.16 extracted from

Jarick, M.; Bertsche, U.; Stahl, M.; Schultz, D.; Methling, K.; Lalk, M.; Stigloher, C.; Steger, M.; Schlosser, A.; Ohlsen, K.
The serine/threonine kinase Stk and the phosphatase Stp regulate cell wall synthesis in Staphylococcus aureus (2018), Sci. Rep., 8, 13693 .

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Cloned(Commentary)

Cloned (Comment)	Organism
gene femX, recombinant expression of N-terminally polyHis-tagged enzyme FemB in Escherichia coli strain BL21(DE3)	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	P0C1Q0	-	-
Staphylococcus aureus NewmanHG	P0C1Q0	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	the lipid II:glycine glycyltransferase FemX can be phosphorylated by the Ser/Thr kinase Stk in vitro. Mass spectrometric analyses identify Thr32, Thr36 and Ser415 as phosphoacceptors. The cognate phosphatase Stp dephosphorylates these phosphorylation sites. Stp was able to completely dephosphorylate these Stk-mediated phosphorylation sites	Staphylococcus aureus

Purification (Commentary)

Purification (Comment)	Organism
recombinant N-terminally polyHis-tagged enzyme FemX from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration	Staphylococcus aureus

Subunits

Subunits	Comment	Organism
homodimer	-	Staphylococcus aureus

Synonyms

Synonyms	Comment	Organism
FemX	-	Staphylococcus aureus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Staphylococcus aureus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Staphylococcus aureus

General Information

General Information	Comment	Organism
metabolism	kinase Stk and phosphatase Stp modulate cell wall synthesis and cell division at several levels. Enzyme FemB interacts with the eukaryotic-like serine/threonine kinase Stk, but is not phosphorylated by it, while the lipid II:glycine glycyltransferase FemX can be phosphorylated by the Ser/Thr kinase Stk in vitro. The cognate phosphatase Stp dephosphorylates these phosphorylation sites. Stk interacts with FemA/B and other cell wall synthesis and cell division proteins, but Stk does not phosphorylate FemA and FemB. Interaction network of Stk, Stp and FemX/A/B proteins among cell wall synthesis and cell division proteins as determined by bacterial two-hybrid analysis, overview	Staphylococcus aureus
physiological function	the bacterial cell envelope is essential for survival and pathogenicity. It forms a barrier against environmental stresses and contributes to virulence and antibiotic resistance. The cell wall of Gram-positive bacteria is composed of a multi-layered mesh of cross-linked peptidoglycan (PGN). PGN consists of chains of repeating disaccharide units comprising N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc). The lactoyl group of MurNAc is supplemented with a penta stem peptide (L-Ala-D-isoGlu-L-Lys-D-Ala-D-Ala). The staphylococcal PGN polysaccharide chains are highly cross-linked via interpeptide bridges of five glycyl residues protruding from the L-lysine of the stem-peptides4. These interpeptide bridges are synthesized by the FemX/A/B enzymes. These non-ribosomal peptidyl-transferases use glycyltRNAs to sequentially add five glycine's to the PGN-lysyl side chain of lipid II. FemX adds the first glycyl unit, FemA the second and third unit, and FemB adds the fourth and fifth glycyl unit to complete the pentaglycine-bridge. Enzyme FemB interacts with the eukaryotic-like serine/threonine kinase Stk, but is not phosphorylated by it. FemA and FemB interact with Stk and with cell wall synthesis enzymes (MurG, Pbp1, Pbp2), Mgt, LytH, RodA, FtsW and cell division proteins (DivIB, DivIC, EzrA). FemA and FemB interact with each other and also form homodimers, which is not the case for FemX. In contrast to FemX, the subsequent enzymes FemA or FemB are non-essential. The essential cell wall synthesis enzyme FemX is a target of Stk and Stp	Staphylococcus aureus

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Release 2023.1 (January 2023)