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PMID:12634338

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Citation

Huard, C, Miranda, G, Wessner, F, Bolotin, A, Hansen, J, Foster, SJ and Chapot-Chartier, MP (2003) Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis. Microbiology (Reading, Engl.) 149:695-705

Abstract

A gene encoding a putative peptidoglycan hydrolase, named acmB, which is a paralogue of the major autolysin acmA gene, was identified in the Lactococcus lactis genome sequence. The acmB gene is transcribed in L. lactis MG1363 and its expression is modulated during cellular growth. The encoded AcmB protein has a modular structure with three domains: an N-terminal domain, especially rich in Ser, Thr, Pro and Asn residues, resembling a cell-wall-associated domain; a central domain homologous to the Enterococcus hirae muramidase catalytic domain; and a C-terminal domain of unknown function. A recombinant AcmB derivative, devoid of its N-terminal domain, was expressed in Escherichia coli. It exhibited hydrolysing activity on the peptidoglycan of several Gram-positive bacteria, including L. lactis. Though showing sequence similarity with enterococcal muramidase, AcmB has N-acetylglucosaminidase specificity. The acmB gene was inactivated in order to evaluate the role of the enzyme. AcmB does not appear to be involved in cell separation but contributes to cellular autolysis.

Links

PubMed Online version:10.1099/mic.0.25875-0

Keywords

Acetylglucosaminidase/chemistry; Acetylglucosaminidase/genetics; Acetylglucosaminidase/metabolism; Amino Acid Sequence; Bacteriolysis; Cloning, Molecular; Escherichia coli/enzymology; Escherichia coli/genetics; Gene Expression Regulation, Bacterial; Lactococcus lactis/enzymology; Lactococcus lactis/genetics; Lactococcus lactis/growth & development; Molecular Sequence Data; N-Acetylmuramoyl-L-alanine Amidase/metabolism; Peptidoglycan/metabolism; Sequence Analysis, DNA

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

9LACT:Q8KKF9

GO:0061784: peptidoglycan N-acetylglucosaminidase activity

ECO:0000314:

F

Figure 5 Analysis by RP-HPLC of the soluble muropeptides released from B. subtilis vegetative cell walls after incubation with AcmB (A) or AcmB and Cellosyl (B). The numbers indicate the peaks analysed by MALDI-TOF mass spectrometry.

complete
CACAO 12201

Notes

See also

References

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