Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
MupG family TIM beta-alpha barrel fold protein
This domain represents the N-terminal domain of 6-phospho-N-acetylmuramidase (MupG) from Staphylococcus aureus [1], also found in putative phospho sugar glycosidases from Gram-negative and -positive species, but mainly firmicutes. MupG [1], specifically cleaves MurNAc 6P-GlcNAc, a product of cell wall turnover, into the sugars MurNAc 6P and GlcNAc, involved in cell wall turnover and recycling. Since some species, for example Lactobacillus plantarum, possess several putative paralogs, the substrate specificity of the proteins containing this domain may not be limited to cell wall sugars, but may include phosphorylated disaccharides in general. Most of these proteins appear to consist of two structural subdomains, as it can be seen in the two available crystal structures of Enterococcus faecalis (PDB:2p0o) and Bacillus cereus (PDB:1X7F). This entry is the larger N-terminal domain that constitutes a TIM-barrel like structure and the C-terminal domain is similar to the cyclophilin family. It should be noted that some proteins lack the C-terminal domain. [1]. 30524387. Recovery of the Peptidoglycan Turnover Product Released by the Autolysin Atl in Staphylococcus aureus Involves the Phosphotransferase System Transporter MurP and the Novel 6-phospho-N-acetylmuramidase MupG. Kluj RM, Ebner P, Adamek M, Ziemert N, Mayer C, Borisova M;. Front Microbiol. 2018;9:2725. (from Pfam)
phospho-sugar glycosidase domain-containing protein
This entry represents the C-terminal domain of 6-phospho-N-acetylmuramidase (MupG) found in bacteria. It characterises putative phospho sugar glycosidases found in Gram-negative and -positive species, but mainly in firmicutes. MupG from Staphylococcus aureus [1], specifically cleaves MurNAc 6P-GlcNAc, a product of cell wall turnover, into the sugars MurNAc 6P and GlcNAc, being involved in cell wall turnover and recycling. Since some species, for example Lactobacillus plantarum, possess several putative paralogs, the substrate specificity of these proteins may not be limited to cell wall sugars, but may include phosphorylated disaccharides in general. Most proteins containing this domain appear to consist of two structural subdomains, as it can be seen in the two available crystal structures of Enterococcus faecalis (PDB:2p0o) and Bacillus cereus (PDB:1X7F). The larger N-terminal domain constitutes a TIM-barrel like structure and the C-terminal domain (this entry) is similar to the cyclophilin family. It should be noted that some proteins lack this domain. [1]. 30524387. Recovery of the Peptidoglycan Turnover Product Released by the Autolysin Atl in Staphylococcus aureus Involves the Phosphotransferase System Transporter MurP and the Novel 6-phospho-N-acetylmuramidase MupG. Kluj RM, Ebner P, Adamek M, Ziemert N, Mayer C, Borisova M;. Front Microbiol. 2018;9:2725. (from Pfam)
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on