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Links from Protein

Items: 10

1.

SH3 domain-containing protein

Date:
2024-08-14
Family Accession:
NF020049.5
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:
2024-10-16
Family Accession:
NF017102.5
Method:
HMM
3.

N-acetylmuramoyl-L-alanine amidase

This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding. This reference shows that the amino terminal region of Swiss:P14892 is required for bacteriolytic activity. [1]. 3070348. Cloning, sequencing and expression of a Bacillus bacteriolytic enzyme in Escherichia coli. Potvin C, Leclerc D, Tremblay G, Asselin A, Bellemare G;. Mol Gen Genet 1988;214:241-248. [2]. 1677905. Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity. Wang X, Wilkinson BJ, Jayaswal RK;. Gene 1991;102:105-109. [3]. 8171031. The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase. Cheng X, Zhang X, Pflugrath JW, Studier FW;. Proc Natl Acad Sci U S A 1994;91:4034-4038. (from Pfam)

GO Terms:
Molecular Function:
N-acetylmuramoyl-L-alanine amidase activity (GO:0008745)
Biological Process:
peptidoglycan catabolic process (GO:0009253)
Date:
2024-10-16
Family Accession:
NF013661.5
Method:
HMM
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.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.

SH3 domain-containing protein

Src Homology 3 (SH3) domain-containing protein plays versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others

Date:
2017-03-02
Family Accession:
11156870
Method:
Sparcle
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