Information on EC 2.3.2.18 - N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase

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The expected taxonomic range for this enzyme is: Staphylococcus

EC NUMBER
COMMENTARY
2.3.2.18
-
RECOMMENDED NAME
GeneOntology No.
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 glycyl-tRNAGly = MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-penta-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 tRNAGly
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Peptidoglycan biosynthesis
-
peptidoglycan cross-bridge biosynthesis I (S. aureus)
-
SYSTEMATIC NAME
IUBMB Comments
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
This Staphylococcus aureus enzyme catalyses the successive transfer of two Gly moieties from charged tRNAs to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphosphoundecaprenyl-GlcNAc, attaching them to the three Gly molecules that were previously attached to the N6 of the L-Lys at position 3 of the pentapeptide by EC 2.3.2.16 (lipid II:glycine glycyltransferase) and EC 2.3.2.17 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase). This is the last step in the synthesis of the pentaglycine interpeptide bridge that is used in this organism for the crosslinking of different glycan strands to each other.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
FemB
D4N302
gene name
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
clinical isolates MRSA252, SA 1306, SA 1326, SA 1552 and SA 4666
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
D4N302
decreased expression of the femB gene leads to reduced methicillin resistance
physiological function
-
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
-
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
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
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i.e. lipid II-Gly3. Enzyme is specific for lipid II-Gly3 as acceptor
-
-
?
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
P95735
calculated
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
95400
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
P95735
x * 49287, calculated
dimer
-
2 * 53400, SDS-PAGE
additional information
-
proteins FemA and FemB form homo- and heterodimers in vitro
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression as His-tagged protein in Escherichia coli
-
expression in Escherichia coli
P95735
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
femB gene expression is not upregulated in oxacillin susceptible methicillin-resistant OS-MRSA strains compared to low- and high-level methicillin-resistant MRSA control strains
D4N302
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
the lysostaphin immunity factor Lif is able to complement lack of FemB by inserting serine for glycine in the side chain. Methicillin resistance, which depends on functional FemA and FemB, is not complemented by Lif suggesting that serine-substituted side-chains are a lesser substrate for penicillin-binding protein PBP2' in methicillin resistance
additional information
-
in strains carrying mutations of FemA, femAB, or the femAX genes, the sorting reaction of surface proteins is significantly slowed. Strains carrying mutations in the fem genes display a decreased rate of surface protein precursor cleavage as compared with the wildtype strains, suggesting that the altered cross-bridges slow the anchoring of surface proteins