Erythromycin esterase and succinoglycan biosynthesis related proteins; This group contains ...
72-435
2.47e-102
Erythromycin esterase and succinoglycan biosynthesis related proteins; This group contains erythromycin esterase, which shares conserved active site residues of the Tiki/TraB family. Erythromycin esterases (EreA and EreB) disrupt erythromycin via the hydrolysis of the macrolactone ring. A critical catalytic histidine acts as a general base in the activation of a water molecule. Macrolides act by inhibiting bacterial protein synthesis by binding at the exit tunnel of ribosomal subunit 50s, blocking the translation of the polypeptide. Erythromycin esterase, typically found in integrons and transposons, confers antibiotic resistance through the disruption of the drug ring structure. EreB substrate profile is substantially broader than that for EreA, being able to also metabolize semisynthetic derivatives such as azalide azithromycin.
Pssm-ID: 350610 Cd Length: 367 Bit Score: 309.32 E-value: 2.47e-102
Erythromycin esterase and succinoglycan biosynthesis related proteins; This group contains ...
72-435
2.47e-102
Erythromycin esterase and succinoglycan biosynthesis related proteins; This group contains erythromycin esterase, which shares conserved active site residues of the Tiki/TraB family. Erythromycin esterases (EreA and EreB) disrupt erythromycin via the hydrolysis of the macrolactone ring. A critical catalytic histidine acts as a general base in the activation of a water molecule. Macrolides act by inhibiting bacterial protein synthesis by binding at the exit tunnel of ribosomal subunit 50s, blocking the translation of the polypeptide. Erythromycin esterase, typically found in integrons and transposons, confers antibiotic resistance through the disruption of the drug ring structure. EreB substrate profile is substantially broader than that for EreA, being able to also metabolize semisynthetic derivatives such as azalide azithromycin.
Pssm-ID: 350610 Cd Length: 367 Bit Score: 309.32 E-value: 2.47e-102
diverse proteins related to the Tiki and TraB protease domains; The extracellular domain of ...
77-174
4.91e-15
diverse proteins related to the Tiki and TraB protease domains; The extracellular domain of Tiki family proteins shares homology with bacterial TraB/PrgY proteins which are known for their roles in the inhibition of mating pheromones. Tiki and TraB/PrgY proteins share limited sequence identity, but their predicted secondary structures reveal that several catalytic residues are anchored in a similar manner, consistent with a common evolutionary origin. Tiki domains are related to the erythromycin esterase, gumN plant pathogens, RtxA toxins, and Campylobacter Jejuni heme-binding, ChaN-like proteins. Tiki is a membrane-associated metalloprotease (MEROPS family M96) that inhibits Wnt via the cleavage of its amino terminus, diminishing Wnt's binding to receptors. Wnt is essential in animal development and homeostasis. In Xenopus, Tiki is critical in head development. In human cells, Tiki inhibits Wnt-signaling, which is important in embryogenesis, homeostasis, and regeneration. Deregulation of Wnt contributes to birth defects, cancer and various diseases. TraB/PrgY protein has been identified in gut bacterium Enterococcus faecalis, but its function has not been well characterized. Plasmid-borne TraB has been implicated in the regulation of pheromone sensitivity and specificity. Based on homology to Tiki activity, it has been proposed that TraB acts as a metalloprotease in the inactivation of mating pheromone. Pasteurella multicida toxin has structural and sequence similarity to the Tiki/TraB family of proteases. However, unlike related multidomain toxins in this family, they do not exhibit conservation of the typical active site residues.
Pssm-ID: 350612 Cd Length: 127 Bit Score: 71.34 E-value: 4.91e-15
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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