|Quickview||Gene||Gene Product(s)||Expression||Evolution||On One Page|
ECK0211, b0211, JW5018, dniR, yafG, yafG
Membrane-bound lytic transglycosylase D, murein hydrolase; periplasmic OM-attached lipoprotein
|Function from GO||
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MltD has been shown to be a murein hydrolase using zymography, to cause lysis or osmotically-stabilized spheroplasts when overproduced, and to be inhibited by bulgecin (Dijkstra A.J., Rudd, K.E., and Keck, W., A new member of the transglycosylase family of Escherichia coli displays a Gram-positive hydrolase motif, in "The soluble lytic transglycolsylase family of Escherichia coli", A.J. Dijkstra, pp. 85-101, Ph.D. thesis, University of Groningen, the Netherlands,1997). MltD has two Gram-positive peptidoglycan-binding motifs in the C-terminus. MltD has a central lysozyme-like domain. MltD should cleave the glycosidic bonds between the N-acetylmuramic acid and N-acetylglucosamine residues in murein. First 15 aa are a type II signal peptide. The proposed DniR function as a regulator of hexaheme nitrite reductase is probably artifactual.
- Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.