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Links from Protein

Items: 7

1.

CW_7 repeat protein

This domain was originally found in the C-terminal moiety of the Cpl-7 lysozyme encoded by the Streptococcus pneumoniae bacteriophage Cp-7 (Swiss:P19385). It is also found in the cell wall hydrolases of human and life-stock pathogens. CW_7 repeats make up a cell wall binding motif [3][4]. [1]. 2311937. Modular organization of the lytic enzymes of Streptococcus. pneumoniae and its bacteriophages.. Garcia P, Garcia JL, Garcia E, Sanchez-Puelles JM, Lopez R;. Gene 1990;86:81-88.. [2]. 15539074. Recent trends on the molecular biology of pneumococcal capsules,. lytic enzymes, and bacteriophage.. Lopez R, Garcia E;. FEMS Microbiol Rev 2004;28:553-580.. [3]. 23056389. Thermal stability of Cpl-7 endolysin from the streptococcus. pneumoniae bacteriophage Cp-7; cell wall-targeting of its CW_7. motifs.. Bustamante N, Rico-Lastres P, Garcia E, Garcia P, Menendez M;. PLoS One. 2012;7:e46654.. [4]. 20720016. Cpl-7, a lysozyme encoded by a pneumococcal bacteriophage with a. novel cell wall-binding motif.. Bustamante N, Campillo NE, Garcia E, Gallego C, Pera B, Diakun. GP, Saiz JL, Garcia P, Diaz JF, Menendez M;. J Biol Chem. 2010;285:33184-33196. (from Pfam)

Date:
2024-08-14
Family Accession:
NF019836.5
Method:
HMM
2.

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:
2024-08-14
Family Accession:
NF017102.5
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.

CHAP domain-containing protein

cysteine, histidine-dependent amidohydrolase/peptidase (CHAP) domain-containing protein may function as an amidase involved in the cleavage of peptidoglycans

Date:
2017-03-02
Family Accession:
11156816
Method:
Sparcle
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