6-phospho-N-acetylmuramidase, N-terminal; This domain represents the N-terminal domain of ...
6-241
6.38e-126
6-phospho-N-acetylmuramidase, N-terminal; This domain represents the N-terminal domain of 6-phospho-N-acetylmuramidase (MupG) from Staphylococcus aureus, also found in putative phospho sugar glycosidases from Gram-negative and -positive species, but mainly firmicutes. MupG, 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.
Pssm-ID: 465993 Cd Length: 235 Bit Score: 361.06 E-value: 6.38e-126
6-phospho-N-acetylmuramidase, N-terminal; This domain represents the N-terminal domain of ...
6-241
6.38e-126
6-phospho-N-acetylmuramidase, N-terminal; This domain represents the N-terminal domain of 6-phospho-N-acetylmuramidase (MupG) from Staphylococcus aureus, also found in putative phospho sugar glycosidases from Gram-negative and -positive species, but mainly firmicutes. MupG, 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.
Pssm-ID: 465993 Cd Length: 235 Bit Score: 361.06 E-value: 6.38e-126
6-phospho-N-acetylmuramidase, C-terminal; This entry represents the C-terminal domain of ...
247-361
1.80e-46
6-phospho-N-acetylmuramidase, C-terminal; This entry represents the C-terminal domain of 6-phospho-N-acetylmuramidase (MupG) found in bacteria. It characterizes putative phospho sugar glycosidases found in Gram-negative and -positive species, but mainly in firmicutes. MupG from Staphylococcus aureus, 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.
Pssm-ID: 461779 Cd Length: 116 Bit Score: 154.26 E-value: 1.80e-46
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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