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Literature summary for 2.3.2.17 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 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.2.17

Cloned(Commentary)

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Staphylococcus aureus
Mn2+ required Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus P0A0A5
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally polyHis-tagged enzyme FemA 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
FemA
-
 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
malfunction a femA deletion leads to accumulation of monoglycine which decreases the interpeptide cross-linking in the peptidoglycan (PGN) sacculus as compared to wild-type cells Staphylococcus aureus
metabolism kinase Stk and phosphatase Stp modulate cell wall synthesis and cell division at several levels. Enzyme FemA 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 FemA 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 Staphylococcus aureus