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Links from Protein

Items: 7

1.

cell wall hydrolase

These enzymes have been implicated in cell wall hydrolysis, most extensively in Bacillus subtilis. For instance Swiss:P50739 is expressed during sporulation as an inactive form and then deposited on the cell outer cortex. During germination the the enzyme is activated and hydrolyses the cortex([1]). A similar role is carried out by the partially redundant Swiss:P42249 ([2]). It is not clear whether these enzymes are amidases or peptidases. [1]. 10658652. Complete spore-cortex hydrolysis during germination of Bacillus subtilis 168 requires SleB and YpeB. Boland FM, Atrih A, Chirakkal H, Foster SJ, Moir A;. Microbiology 2000;146:57-64. [2]. 9515903. Regulation and characterization of a newly deduced cell wall hydrolase gene (cwlJ) which affects germination of Bacillus subtilis spores. Ishikawa S, Yamane K, Sekiguchi J;. J Bacteriol 1998;180:1375-1380. (from Pfam)

GO Terms:
Molecular Function:
hydrolase activity (GO:0016787)
Date:
2024-10-16
Family Accession:
NF019128.5
Method:
HMM
2.

peptidoglycan-binding protein

This domain is composed of three alpha helices [1]. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation [2]. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins [3]. The domain is found to bind peptidoglycan experimentally [4]. This paper gives the crystal structure for this domain. However no function is given for this domain. [1]. 7121588. Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution. Dideberg O, Charlier P, Dive G, Joris B, Frere JM, Ghuysen JM;. Nature 1982;299:469-470. [2]. 1683402. Cloning, expression, sequence analysis and biochemical characterization of an autolytic amidase of Bacillus subtilis 168 trpC2. Foster SJ;. J Gen Microbiol 1991;137:1987-1998. [3]. 7656014. The NMR structure of the inhibited catalytic domain of human stromelysin-1. Gooley PR, O'Connell JF, Marcy AI, Cuca GC, Salowe SP, Bush BL, Hermes JD, Esser CK, Hagmann WK, Springer JP, et al;. Nat Struct Biol 1994;1:111-118. [4]. 17697255. Muralytic activity and modular structure of the endolysins of Pseudomonas aeruginosa bacteriophages phiKZ and EL. Briers Y, Volckaert G, Cornelissen A, Lagaert S, Michiels CW, Hertveldt K, Lavigne R;. Mol Microbiol. 2007;65:1334-1344. (from Pfam)

Date:
2024-10-16
Family Accession:
NF013625.5
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.

spore cortex-lytic enzyme

Members of this protein family are the spore cortex-lytic enzyme SleB from Bacillus subtilis and other Gram-positive, endospore-forming bacterial species. This protein is stored in an inactive form in the spore and activated during germination.

Gene:
sleB
GO Terms:
Molecular Function:
catalytic activity (GO:0003824)
Biological Process:
spore germination (GO:0009847)
Date:
2021-04-27
Family Accession:
TIGR02869.1
Method:
HMM
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