Protein Family Models

Described members of this protein family occur at the tip of tails of phi-29-like phage. The location suggests both lysozyme activity, as supported by the lysozyme-like fold, and a page morphogenetic function, consistent with experimental observations, as location at the tail tip could be important for plugging the tail tube and ensuring proper phage assembly.

Date:

2024-04-03

This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78 [1]. This domain is found to be the catalytic domain of PlyCA [4]. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyses the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine [5]. [1]. 7775463. Glutathionylspermidine metabolism in Escherichia coli.. Purification, cloning, overproduction, and characterization of a. bifunctional glutathionylspermidine synthetase/amidase.. Bollinger JM Jr, Kwon DS, Huisman GW, Kolter R, Walsh CT;. J Biol Chem 1995;270:14031-14041.. [2]. 12765834. The CHAP domain: a large family of amidases including GSP. amidase and peptidoglycan hydrolases.. Bateman A, Rawlings ND;. Trends Biochem Sci 2003;28:234-237.. [3]. 12765833. Amidase domains from bacterial and phage autolysins define a. family of gamma-D,L-glutamate-specific amidohydrolases.. Rigden DJ, Jedrzejas MJ, Galperin MY;. Trends Biochem Sci 2003;28:230-234.. [4]. 16818874. PlyC: a multimeric bacteriophage lysin.. Nelson D, Schuch R, Chahales P, Zhu S, Fischetti VA;. Proc Natl Acad Sci U S A. 2006;103:10765-10770.. [5]. 21226054. Structure and mechanism of Escherichia coli. glutathionylspermidine amidase belonging to the family of. cysteine; histidine-dependent amidohydrolases/peptidases.. Pai CH, Wu HJ, Lin CH, Wang AH;. Protein Sci. 2011;20:557-566. (from Pfam)

Date:

2024-04-03