Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.2.16 gene femX, recombinant expression of N-terminally polyHis-tagged enzyme FemB in Escherichia coli strain BL21(DE3) Staphylococcus aureus
2.3.2.17 gene femA, recombinant expression of N-terminally polyHis-tagged enzyme FemA in Escherichia coli strain BL21(DE3) Staphylococcus aureus
2.3.2.18 gene femB, recombinant expression of N-terminally polyHis-tagged enzyme FemB in Escherichia coli strain BL21(DE3) Staphylococcus aureus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.3.2.17 Mg2+ required Staphylococcus aureus
2.3.2.17 Mn2+ required Staphylococcus aureus
2.3.2.18 Mg2+ required Staphylococcus aureus
2.3.2.18 Mn2+ required Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.16 Staphylococcus aureus P0C1Q0
-
-
2.3.2.16 Staphylococcus aureus NewmanHG P0C1Q0
-
-
2.3.2.17 Staphylococcus aureus P0A0A5
-
-
2.3.2.18 Staphylococcus aureus P0A0A8
-
-
2.3.2.18 Staphylococcus aureus NewmanHG P0A0A8
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.3.2.16 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)

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

Subunits

EC Number Subunits Comment Organism
2.3.2.16 homodimer
-
 Staphylococcus aureus
2.3.2.17 homodimer
-
 Staphylococcus aureus
2.3.2.18 homodimer
-
 Staphylococcus aureus

Synonyms

EC Number Synonyms Comment Organism
2.3.2.16 FemX
-
 Staphylococcus aureus
2.3.2.17 FemA
-
 Staphylococcus aureus
2.3.2.18 FemB
-
 Staphylococcus aureus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.2.16 37
-
 assay at Staphylococcus aureus
2.3.2.17 37
-
 assay at Staphylococcus aureus
2.3.2.18 37
-
 assay at Staphylococcus aureus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.2.16 7.5
-
 assay at Staphylococcus aureus
2.3.2.17 7.5
-
 assay at Staphylococcus aureus
2.3.2.18 7.5
-
 assay at Staphylococcus aureus

General Information

EC Number General Information Comment Organism
2.3.2.16 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
2.3.2.16 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
2.3.2.17 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
2.3.2.17 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
2.3.2.17 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
2.3.2.18 malfunction a femB deletion leads to accumulation of triglycine which decreases the interpeptide cross-linking in the peptidoglycan (PGN) sacculus as compared to wild-type cells Staphylococcus aureus
2.3.2.18 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. FemX interacts neither with Stk, Stp, FemA nor FemB. But FemX interacts weakly with Pbp2, RodA, DivIC and EzrA. 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
2.3.2.18 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 Staphylococcus aureus