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Literature summary for 3.4.16.4 extracted from

  • Moell, A.; Doerr, T.; Alvarez, L.; Davis, B.M.; Cava, F.; Waldor, M.K.
    A D, D-carboxypeptidase is required for Vibrio cholerae halotolerance (2015), Environ. Microbiol., 17, 527-540.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Vibrio cholerae Q9KTF5
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Vibrio cholerae ATCC 39315 Q9KTF5
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Synonyms

Synonyms Comment Organism
DacA-1
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Vibrio cholerae
VC_0947
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Vibrio cholerae

General Information

General Information Comment Organism
physiological function Vibrio cholerae lacking isoform DacA-1 displays slow growth, aberrant morphology and altered peptidoglycan homeostasis in Luria-Bertani medium, as well as a profound plating defect. DacA-1 alone among Vibrio cholerae’s low molecular weight penicillin-binding proteins is critical for bacterial growth. The growth and morphology of the dacA-1 mutant are unimpaired in Luria-Bertani media containing reduced concentrations of NaCl of 100 mM or less, and also within suckling mice, a model host for the study of cholera pathogenesis. Peptidoglycan from the dacA-1 mutant contains elevated pentapeptidelevels in standard and low salt media Vibrio cholerae