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Links from Protein

Items: 8

1.

CHAP domain-containing protein

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:
2024-10-16
Family Accession:
NF017102.5
Method:
HMM
2.

LysM peptidoglycan-binding domain-containing protein

The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation [1]. This domain may have a general peptidoglycan binding function. The structure of this domain is known [2]. [1]. 1352512. Modular design of the Enterococcus hirae muramidase-2 and Streptococcus faecalis autolysin. Joris B, Englebert S, Chu CP, Kariyama R, Daneo-Moore L, Shockman GD, Ghuysen JM;. FEMS Microbiol Lett 1992;70:257-264. [2]. 10843862. The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). Bateman A, Bycroft M;. J Mol Biol 2000;299:1113-1119. (from Pfam)

Date:
2024-10-29
Family Accession:
NF013630.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

LysM and COG3942 domain-containing protein

LysM and COG3942 domain-containing protein

Date:
2019-03-21
Family Accession:
13291756
Method:
Sparcle
8.

autolysin/adhesin Aaa

Aaa (autolysin/adhesin as found in Staphylococcus aureus) is a multifunctional protein with both autolytic and host extracellular matrix-binding activities.

Gene:
aaa
Date:
2019-01-14
Family Accession:
NBR007890
Method:
BlastRule
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