Reviewed,
UniProtKB/Swiss-Prot P03706 (LYS_LAMBD)
Last modified
June 16, 2009.
Version 68.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Lysozyme EC=3.2.1.17 Alternative name(s): Lysis protein Muramidase Endolysin | ||
| Gene names |
| ||
| Organism | Enterobacteria phage lambda (Bacteriophage lambda) | ||
| Taxonomic identifier | 10710 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Caudovirales › Siphoviridae › Lambda-like viruses | ||
| Virus host | Escherichia coli [TaxID: 562] |
Protein attributes
| Sequence length | 158 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity. Acts as a transglycosylase. Cleaves glycosidic bonds between the C1 of N-acetyl muramic acids (NAM) and C4 of N-acetyl glucosamines (NAG) of the peptidoglycan of the bacterial walls. |
| Catalytic activity | Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. |
| Subunit structure | Monomer. |
| Sequence similarities | Belongs to the glycosyl hydrolase 24 family. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro cytolysisInferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic processInferred from electronic annotation. Source: InterPro |
| Molecular function | lysozyme activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 158 | 158 | Lysozyme | PRO_0000218108 | ||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||
| Active site | 19 | 1 | ||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||
| Sequence conflict | 74 | 1 | Missing AA sequence Ref.2 | |||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||
| Helix | 6 – 18 | 13 | ||||||||||||||||||||||||||||||
| Beta strand | 21 – 26 | 6 | ||||||||||||||||||||||||||||||
| Turn | 31 – 34 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 53 – 56 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 59 – 61 | 3 | ||||||||||||||||||||||||||||||
| Turn | 65 – 68 | 4 | ||||||||||||||||||||||||||||||
| Helix | 71 – 81 | 11 | ||||||||||||||||||||||||||||||
| Helix | 88 – 101 | 14 | ||||||||||||||||||||||||||||||
| Helix | 105 – 110 | 6 | ||||||||||||||||||||||||||||||
| Helix | 113 – 120 | 8 | ||||||||||||||||||||||||||||||
| Turn | 121 – 123 | 3 | ||||||||||||||||||||||||||||||
| Helix | 135 – 148 | 14 | ||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequence of bacteriophage lambda DNA." Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B. J. Mol. Biol. 162:729-773(1982) [PubMed: 6221115] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "Amino-acid sequence of lambda phage endolysin." Imada M., Tsugita A. Nature New Biol. 233:230-231(1971) Cited for: PROTEIN SEQUENCE. |
| [3] | "Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes." Evrard C., Fastrez J., Declercq J.-P. J. Mol. Biol. 276:151-164(1998) [PubMed: 9514719] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| J02459 Genomic DNA. Translation: AAA96598.1. | |||||||||||||||||||||||||
| PIR | EYBPL. B04333. | ||||||||||||||||||||||||
| RefSeq | NP_040645.1. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||
Protein family/group databases | |||||||||||||||||||||||||
| CAZy | GH104. Glycoside Hydrolase Family 104. | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| GeneID | 2703480. | ||||||||||||||||||||||||
| GenomeReviews | Gene locus lambdap76 in contig J02459_GR. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| BRENDA | 3.2.1.17. 96374. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR002196. Glyco_hydro_24. [Graphical view] | ||||||||||||||||||||||||
| Pfam | PF00959. Phage_lysozyme. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | LYS_LAMBD | ||||||||
| Accession | Primary (citable) accession number: P03706 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


