Nomenclature
EC number
2.3.2.18
Systematic name
N-acetylmuramoyl-l-alanyl-d-glutamyl-l-lysyl-(N6-triglycine)-d-alanyl-dalanine-diphospho-ditrans,octacis-undecaprenyl-N-acetylglucosamine:glycine glycyltransferas
Recommended name
N-acetylmuramoyl-l-alanyl-d-glutamyl-l-lysyl-(N6-triglycine)-d-alanyl-dalanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
Synonyms
FemB <1,2> [2,6]
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References
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)
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)
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)
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)
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)
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)
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Schomburg, D., Schomburg, I. (2013). N-acetylmuramoyl-l-alanyl-d-glutamyl-l-lysyl-(N6-triglycine)-d-alanyl-d-alaninediphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase 2.3.2.18. In: Schomburg, D., Schomburg, I. (eds) Class 2–3.2 Transferases, Hydrolases. Springer Handbook of Enzymes. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-36240-8_44
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