NEAT domain-containing leucine-rich repeat protein. Members of this family have an N-terminal NEAT (near transporter) domain often associated with iron transport, followed by a leucine-rich repeat region with significant sequence similarity to the internalins of Listeria monocytogenes. However, since Bacillus cereus (from which this protein was described, in PMID:16978259) is not considered an intracellular pathogen, and the function may be iron transport rather than internalization, applying the name "internalin" to this family probably would be misleading.

Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.

glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.

NEAT domain-containing leucine-rich repeat protein. Members of this family have an N-terminal NEAT (near transporter) domain often associated with iron transport, followed by a leucine-rich repeat region with significant sequence similarity to the internalins of Listeria monocytogenes. However, since Bacillus cereus (from which this protein was described, in PMID:16978259) is not considered an intracellular pathogen, and the function may be iron transport rather than internalization, applying the name "internalin" to this family probably would be misleading.

S-layer homology domain.

Crystalstructure of the SLH domain of Sap from Bacillus anthracis in complex with a pyruvylated SCWP unit [Bacillus anthracis]

Thestructure of the SLH domain from B. anthracis surface array protein at 1.8A [Bacillus anthracis]

Structureof the SbsB S-layer protein of Geobacillus stearothermophilus PV72p2 in complex with nanobody KB6 [Geobacillus stearothermophilus]

Structureof the SbsB S-layer protein of Geobacillus stearothermophilus PV72p2 in complex with nanobody KB6 [Geobacillus stearothermophilus]

Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2

Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1

Endoglucanase OS=Bacillus sp. (strain KSM-635) OX=1415 PE=1 SV=1

Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1

Surface-layer 125 kDa protein OS=Lysinibacillus sphaericus OX=1421 PE=3 SV=1