2.3.2.17: N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
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Reaction
+ 2 glycyl-tRNAGly = + 2 tRNAGly
Synonyms
FemA
ECTree
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Engineering
Engineering on EC 2.3.2.17 - N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
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additional information
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analysis of several related methicillin-resistant, methicillin-susceptible, and TnS51 insertionally inactivated femA mutants. All mutants have a reduced peptidoglycan glycine content compared to that of related femA parent strains. Additional effects of femA inactivation and the subsequent decrease in peptidoglycan-associated glycine are reduced digestion of peptidoglycan by recombinant lysostaphin, unaltered digestion of peptidoglycan by Chalaropsis B-muramidase, reduced cell wall turnover, reduced whole-cell autolysis, and increased sensitivity towards beta-lactam antibiotics. The peptidoglycan-associated glycine content of a femA::Tn5Sl methicillin-susceptible strain is restored concomitantly with the methicillin resistance to a level almost equal to that of its femA4 methicillin-resistant parent strain by introduction of a plasmid encoding femA
additional information
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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
additional information
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the lysostaphin immunity factor Lif is not able to complement lack of FemA by inserting serine for glycine in the side chain. Methicillin resistance, which depends on functional FemA and FemB, is neither complemented by Lif