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MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + glycyl-tRNAGly
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-penta-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + tRNAGly
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-triglycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 glycyl-tRNA
N-acetylmuramoyl-L-alanyl-D-isoglutaminyl-L-lysyl-(N6-pentaglycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine + 2 tRNA
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i.e. lipid II-Gly3. Enzyme is specific for lipid II-Gly3 as acceptor
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MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + glycyl-tRNAGly
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-penta-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + tRNAGly
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MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + glycyl-tRNAGly
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-penta-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + tRNAGly
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MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + glycyl-tRNAGly
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-penta-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + tRNAGly
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + glycyl-tRNAGly
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-penta-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + tRNAGly
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MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + glycyl-tRNAGly
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-penta-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + tRNAGly
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malfunction
decreased expression of the femB gene leads to reduced methicillin resistance
malfunction
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a Staphylococcus carnosus femB deletion mutant is affected in growth and shows pleiotropic effects such as enhanced methicillin sensitivity, lysostaphin resistance, cell clustering, and decreased peptidoglycan crosslinking
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
malfunction
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a Staphylococcus carnosus femB deletion mutant is affected in growth and shows pleiotropic effects such as enhanced methicillin sensitivity, lysostaphin resistance, cell clustering, and decreased peptidoglycan crosslinking
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malfunction
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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
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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
metabolism
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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
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physiological function
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FemB catalyzes the third step in the synthesis of the pentaglycine interpeptide bridge crosslinking different glycan strands in Staphylococcus aureus. FemX adds the first glycine residue to MurNAc-L-Ala-D-Glu-(N6-Gly)L-Lys-D-Ala-D-Ala-diphosphoundecaprenyl-M-acetylglucosamine, i.e. lipid II. Addition of glycine residues 2, 3 and glycine residues 4, 5 is catalyzed by enzymes FemA and FemB, respectively. None of the FemABX enzymes requires the presence of one or two of the other Fem proteins for activity, rather, bridge formation is delayed in an in vitro system when all 3 enzymes are present
physiological function
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FemB is involved in the addition of exclusively glycine residues 4 and 5 to the staphylococcal interpeptide bridge. femA mutants leading to truncated proteins still produce intact FemB while exhibiting a phenotype identical to femAB double mutants, such as same muropeptide pattern. FemA is essential for the addition of glycine residues 2 and 3 only to the staphylococcal interpeptide bridge, and FemB cannot substitute for FemA
physiological function
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surface protein is linked to tri- and monoglycyl cross-bridges of peptidoglycan isolated from femB and femA mutant staphylococci, respectively. Peptidoglycan analysis of a femAB mutant strain reveals the presence of pentaglycyl, tetraglycyl-monoseryl, and monoglycyl as well as small amounts of triglycyl cross-bridges. Analysis of anchor peptides shows that surface proteins are mostly linked to tetraglycylmonoseryl as well as pentaglycyl. The sortase activity of Staphylococcus aureus prefers cross-bridges containing five residues, but altered cell-wall cross-bridges can be linked to the COOH-terminal end of surface proteins
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
physiological function
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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
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Tschierske, M.; Ehlert, K.; Stranden, A.M.; Berger-Bachi, B.
Lif, the lysostaphin immunity factor, complements FemB in staphylococcal peptidoglycan interpeptide bridge formation
FEMS Microbiol. Lett.
153
261-264
1997
Staphylococcus aureus
brenda
Alborn, W.E., Jr.; Hoskins, J.; Unal, S.; Flokowitsch, J.E.; Hayes, C.A.; Dotzlaf, J.E.; Yeh, W.K.; Skatrud, P.L.
Cloning and characterization of femA and femB from Staphylococcus epidermidis
Gene
180
177-181
1996
Staphylococcus epidermidis (P95735)
brenda
Ehlert, K.; Schroder, W.; Labischinski, H.
Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation
J. Bacteriol.
179
7573-7576
1997
Staphylococcus aureus
brenda
Ton-That, H.; Labischinski, H.; Berger-Bachi, B.; Schneewind, O.
Anchor structure of staphylococcal surface proteins. III. Role of the FemA, FemB, and FemX factors in anchoring surface proteins to the bacterial cell wall
J. Biol. Chem.
273
29143-29149
1998
Staphylococcus aureus
brenda
Rohrer, S.; Berger-Bachi, B.
Application of a bacterial two-hybrid system for the analysis of protein-protein interactions between FemABX family proteins
Microbiology
149
2733-2738
2003
Staphylococcus aureus
brenda
Schneider, T.; Senn, M.M.; Berger-Bachi, B.; Tossi, A.; Sahl, H.G.; Wiedemann, I.
In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus
Mol. Microbiol.
53
675-685
2004
Staphylococcus aureus
brenda
Giannouli, S.; Labrou, M.; Kyritsis, A.; Ikonomidis, A.; Pournaras, S.; Stathopoulos, C.; Tsakris, A.
Detection of mutations in the FemXAB protein family in oxacillin-susceptible mecA-positive Staphylococcus aureus clinical isolates
J. Antimicrob. Chemother.
65
626-633
2010
Staphylococcus aureus (D4N302)
brenda
Nega, M.; Dube, L.; Kull, M.; Ziebandt, A.K.; Ebner, P.; Albrecht, D.; Krismer, B.; Rosenstein, R.; Hecker, M.; Goetz, F.
Secretome analysis revealed adaptive and non-adaptive responses of the Staphylococcus carnosus femB mutant
Proteomics
15
1268-1279
2015
Staphylococcus carnosus, Staphylococcus carnosus TM300
brenda
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
Sci. Rep.
8
13693
2018
Staphylococcus aureus (P0A0A8), Staphylococcus aureus NewmanHG (P0A0A8)
brenda