|Function||tRNA threonylcarbamoyl adenosine modification protein YgjD|
|Domain Trusted Cutoff||296.10|
|Domain Noise Cutoff||287.85|
|Mainrole Category||Unknown function|
|Entry Date||Mar 18 2009 10:07AM|
|Last Modified||Aug 12 2012 6:56PM|
|Comment||This model represents bacterial members of a protein family that is widely distributed. In a few pathogenic species, the protein is exported in a way that may represent an exceptional secondary function. This model plus companion (archaeal) model TIGR03722 together span the prokaryotic member sequences of TIGR00329, a protein family that appears universal in life, and whose broad function is unknown. A member of TIGR03722 has been characterized as a DNA-binding protein with apurinic endopeptidase activity. In contrast, the rare characterized members of the present family show O-sialoglycoprotein endopeptidase (EC. 126.96.36.199) activity after export. These include glycoprotease (gcp) from Pasteurella haemolytica A1 and a cohemolysin from Riemerella anatipestifer (GB|AAG39646.1). The member from Staphylococcus aureus is essential and is related to cell wall dynamics and the modulation of autolysis, but members are also found in the Mycoplasmas (which lack a cell wall). A reasonable hypothesis is that virulence-related activities after export are secondary to a bacterial domain-wide unknown function.|
RT Biosynthesis of Threonylcarbamoyl Adenosine (t6A), a Universal tRNA Nucleoside.
RA Deutsch C, El Yacoubi B, de Crecy-Lagard V, Iwata-Reuyl D
RL J Biol Chem. 2012 Apr 20;287(17):13666-73.
RT Conditional mutation of an essential putative glycoprotease eliminates autolysis in Staphylococcus aureus.
RA Zheng L, Yu C, Bayles K, Lasa I, Ji Y
RL J Bacteriol. 2007 Apr;189(7):2734-42.
RT Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene.
RA Abdullah KM, Lo RY, Mellors A
RL J Bacteriol. 1991 Sep;173(18):5597-603.|
|Genome Property||GenProp0799: bacterial core gene set, exactly 1 per genome (HMM)|
| ||GenProp1060: tRNA N6-threonylcarbamoyladenosine modification (HMM)|
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