Reviewed,
UniProtKB/Swiss-Prot P59206 (LYTB_STRR6)
Last modified
September 1, 2009.
Version 49.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative endo-beta-N-acetylglucosaminidase EC=3.2.1.96 Alternative name(s): Murein hydrolase | ||||
| Gene names |
| ||||
| Organism | Streptococcus pneumoniae (strain ATCC BAA-255 / R6) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 171101 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus |
Protein attributes
| Sequence length | 702 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Plays an important role in cell wall degradation and cell separation. |
| 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. |
| Subcellular location | Secreted By similarity. |
| Sequence similarities | Belongs to the glycosyl hydrolase 73 family. Contains 15 cell wall-binding repeats. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell wall biogenesis/degradation |
| Cellular component | Secreted |
| Domain | Repeat Signal |
| Molecular function | Hydrolase |
| Technical term | Complete proteome Direct protein sequencing |
| 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 – 23 | 23 | Ref.1 | ||||||
| Chain | 24 – 702 | 679 | Putative endo-beta-N-acetylglucosaminidase | PRO_0000012117 | |||||
Regions | |||||||||
| Repeat | 42 – 63 | 22 | Cell wall-binding 1 | ||||||
| Repeat | 65 – 84 | 20 | Cell wall-binding 2 | ||||||
| Repeat | 86 – 105 | 20 | Cell wall-binding 3 | ||||||
| Repeat | 124 – 145 | 22 | Cell wall-binding 4 | ||||||
| Repeat | 147 – 166 | 20 | Cell wall-binding 5 | ||||||
| Repeat | 185 – 206 | 22 | Cell wall-binding 6 | ||||||
| Repeat | 208 – 227 | 20 | Cell wall-binding 7 | ||||||
| Repeat | 229 – 248 | 20 | Cell wall-binding 8 | ||||||
| Repeat | 250 – 271 | 22 | Cell wall-binding 9 | ||||||
| Repeat | 273 – 292 | 20 | Cell wall-binding 10 | ||||||
| Repeat | 294 – 315 | 22 | Cell wall-binding 11 | ||||||
| Repeat | 317 – 336 | 20 | Cell wall-binding 12 | ||||||
| Repeat | 338 – 359 | 22 | Cell wall-binding 13 | ||||||
| Repeat | 361 – 380 | 20 | Cell wall-binding 14 | ||||||
| Repeat | 382 – 403 | 22 | Cell wall-binding 15 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "LytB, a novel pneumococcal murein hydrolase essential for cell separation." Garcia P., Gonzalez M.P., Garcia E., Lopez R., Garcia J.L. Mol. Microbiol. 31:1275-1281(1999) [PubMed: 10096093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-30. |
| [2] | Garcia J. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| [3] | "Genome of the bacterium Streptococcus pneumoniae strain R6." Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., Lee L.N. Glass J.I.J. Bacteriol. 183:5709-5717(2001) [PubMed: 11544234] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AJ010312 Genomic DNA. Translation: CAA09078.2. AE007317 Genomic DNA. Translation: AAK99671.1. Different initiation. | |
| PIR | C97980. |
| RefSeq | NP_358461.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GVM based on UniProtKB P06653. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P59206. |
Protein family/group databases | |
| CAZy | GH73. Glycoside Hydrolase Family 73. |
Genome annotation databases | |
| GeneID | 934406. |
| GenomeReviews | Gene locus spr0867 in contig AE007317_GR. |
| KEGG | spr:spr0867. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P59206. |
Enzyme and pathway databases | |
| BioCyc | SPNE171101:SPR0867-MON. |
Family and domain databases | |
| InterPro | IPR018337. Cell_wall/Cho-bd_repeat. IPR002479. Cell_wall_bd_put. IPR013338. Lyz2. IPR002901. Mano_Glyc_endo_b_GlcNAc. [Graphical view] |
| Pfam | PF01473. CW_binding_1. 12 hits. PF01832. Glucosaminidase. 1 hit. [Graphical view] |
| SMART | SM00047. LYZ2. 1 hit. [Graphical view] |
| PROSITE | PS51170. CW. 15 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LYTB_STRR6 | ||||||||
| Accession | Primary (citable) accession number: P59206 Secondary accession number(s): Q9Z4P7 | ||||||||
| 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
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


