Reviewed,
UniProtKB/Swiss-Prot P39848 (LYTD_BACSU)
Last modified
June 16, 2009.
Version 71.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Beta-N-acetylglucosaminidase EC=3.2.1.96 | ||||||
| Gene names |
| ||||||
| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 880 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Cell wall hydrolase not involved in cell autolysis. It hydrolyzes the beta-1,4 glycan bond between the N-acetylglucosaminyl and the N-acetylmuramoyl residues in the glycan chain. |
| Catalytic activity | Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)2)Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Sequence similarities | Belongs to the glycosyl hydrolase 73 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell wall biogenesis/degradation |
| Cellular component | Secreted |
| Domain | Repeat Signal |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW cellular cell wall macromolecule metabolic processInferred from electronic annotation. Source: InterPro peptidoglycan catabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | amidase activity Inferred from electronic annotation. Source: InterPro mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 27 | 27 | Potential | ||||||
| Chain | 28 – 880 | 853 | Beta-N-acetylglucosaminidase | PRO_0000012118 | |||||
Regions | |||||||||
| Repeat | 439 – 473 | 35 | 1 | ||||||
| Repeat | 479 – 513 | 35 | 2 | ||||||
| Compositional bias | 72 – 75 | 4 | Poly-Thr | ||||||
| Compositional bias | 337 – 340 | 4 | Poly-Lys | ||||||
| Compositional bias | 568 – 571 | 4 | Poly-Ala | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The gene of the N-acetylglucosaminidase, a Bacillus subtilis 168 cell wall hydrolase not involved in vegetative cell autolysis." Margot P., Maueel C., Karamata D. Mol. Microbiol. 12:535-545(1994) [PubMed: 7934877] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "Glucosaminidase of Bacillus subtilis: cloning, regulation, primary structure and biochemical characterization." Rashid M.H., Mori M., Sekiguchi J. Microbiology 141:2391-2404(1995) [PubMed: 7581999] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / AC327. |
| [3] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| U02562 Genomic DNA. Translation: AAA67857.1. D45048 Genomic DNA. Translation: BAA08089.1. AL009126 Genomic DNA. Translation: CAB15595.1. | |
| PIR | S60137. |
| RefSeq | NP_391459.1. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH73. Glycoside Hydrolase Family 73. |
Genome annotation databases | |
| GeneID | 936822. |
| GenomeReviews | Gene locus BSU35780 in contig AL009126_GR. |
| KEGG | bsu:BSU35780. |
| NMPDR | fig|224308.1.peg.3585. |
Organism-specific databases | |
| SubtiList | BG10455. lytD. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P39848. |
| OMA | P39848. GAYDSNP. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU3576-MON. |
| BRENDA | 3.2.1.96. 150. |
Family and domain databases | |
| InterPro | IPR013338. Lyz2. IPR002901. Mano_Glyc_endo_b_GlcNAc. IPR013247. SH3_3. IPR003646. SH3_bac. IPR007730. Spore_cell-division_bac. [Graphical view] |
| Pfam | PF01832. Glucosaminidase. 1 hit. PF08239. SH3_3. 1 hit. PF05036. SPOR. 1 hit. [Graphical view] |
| SMART | SM00047. LYZ2. 1 hit. SM00287. SH3b. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LYTD_BACSU | ||||||||
| Accession | Primary (citable) accession number: P39848 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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