Domains within Bacillus subtilis subsp. subtilis str. 168 protein LYTD_BACSU (P39848)

Beta-N-acetylglucosaminidase

Alternative representations: 1 /

Protein length880 aa
Source databaseUniProt
Identifiers A0A164VED5_BACIU, A0A164VED5, A0A1D8FMT6_BACIU, A0A1D8FMT6, L8AVN5_BACIU, L8AVN5, LYTD_BACSU, P39848

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

This domain architecture was probably invented with the emergence of Bacillus subtilis

Predicted functional partners

LYTD_BACSU is shown as lytD in the network

Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.

The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for lytD

Protein LYTD_BACSU is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map00511Other glycan degradation iPath3
Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

KONameDescription
K23989lytD, lytBmannosyl-glycoprotein endo-beta-N-acetylglucosaminidase [EC:3.2.1.96]

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 224308.BSU35780 in eggNOG.

OGTaxonomic classDescription
6XJRFAll organisms (root)mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase [EC:3.2.1.96],bifunctional autolysin [EC:3.5.1.28 3.2.1.96],N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28]
COG4193Bacteria (superkingdom)mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase [EC:3.2.1.96],bifunctional autolysin [EC:3.5.1.28 3.2.1.96],N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28]
9W0M2Firmicutes (phylum)mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase [EC:3.2.1.96]
G59C0Bacilli (class)mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase [EC:3.2.1.96]
F34EBBacillales (order)mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase [EC:3.2.1.96]
F5ZR0Bacillaceae (family)mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase [EC:3.2.1.96]
AADPMBacillus (genus)mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase [EC:3.2.1.96]

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: