An ampD gene in Pseudomonas aeruginosa encodes a negative regulator of AmpC beta-lactamase expression.
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P. aeruginosa ampD complements E. coli ampD mutants for repression of beta-lactamase expression.
"The ampD product transcomplemented Escherichia coli ampD mutants to wild-type beta-lactamase expression."
Reactions of the three AmpD enzymes of Pseudomonas aeruginosa.
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Purified AmpD hydrolyses only 1,6-anhydromuramyl peptides, the cytoplasmic recycling metabolites.
"AmpD is the true protease for the recycling process in P. aeruginosa, as its function is exclusive for turnover of 1,6-anhydromuramyl variants 4–6"
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AmpD is the cytoplasmic enzyme of the three paralogues.
"This analysis identifies AmpD of P. aeruginosa as the cytoplasmic protease for commitment to the cell-wall recycling events and for the reversal of the activation of the antibiotic-resistance pathway."
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The reaction is hydrolysis of the amide bond to the lactyl moiety.
"the nature of the enzymatic reaction of AmpD with this compound is hydrolysis of the amide bond to the lactyl moiety"
UniProtKB P13016 (E. coli AmpD), fetched 2026-11-05 by fetch_comparators.sh
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E. coli AmpD, the experimental seed of PTN001252273 and a leaf of PTN002019137, is cytoplasmic.
"SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:19309146}."
UniProtKB P75820 (E. coli AmiD), fetched 2026-11-05 by fetch_comparators.sh
Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods