Literature summary for 2.7.8.33 extracted from

Amer, A.O.; Valvano, M.A.
Conserved amino acid residues found in a predicted cytosolic domain of the lipopolysaccharide biosynthetic protein WecA are implicated in the recognition of UDP-N-acetylglucosamine (2001), Microbiology, 147, 3015-3025.

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Cloned(Commentary)

Cloned (Comment)	Organism
design of a vector system to generate C-terminal protein fusions to the FLAG epitope, which is used to find conditions to monitor WecA by immunoblot analysis with anti-FLAG antibodies, to determine the correct site for initiation of translation, and to investigate the localization of hybrid proteins in the cytoplasmic membrane	Escherichia coli
detailed examination of the role of a conserved motif within the predicted large cytosolic loop	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	design of a vector system to generate C-terminal protein fusions to the FLAG epitope, which is used to find conditions to monitor WecA by immunoblot analysis with anti-FLAG antibodies, to determine the correct site for initiation of translation, and to investigate the localization of hybrid proteins in the cytoplasmic membrane	Escherichia coli	16020	-
membrane	modelling of the topology of WecA taking into account the available experimental data from the topological analysis of MraY	Escherichia coli	16020	-

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AC78	-	-

Synonyms

Synonyms	Comment	Organism
GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase	-	Escherichia coli
Rfe	-	Escherichia coli
UDP-N-acetylglucosamine:undecaprenyl-phosphate GlcNAc-1-phosphate transferase	-	Escherichia coli
WecA	-	Escherichia coli

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Release 2023.1 (January 2023)