Reviewed,
UniProtKB/Swiss-Prot Q37875 (LYS_BPP1)
Last modified
June 16, 2009.
Version 56.
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 Protein gp17 | ||||
| Gene names |
| ||||
| Organism | Enterobacteria phage P1 (Bacteriophage P1) | ||||
| Taxonomic identifier | 10678 [NCBI] | ||||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Caudovirales › Myoviridae › P1-like viruses | ||||
| Virus host | Enterobacteriaceae [TaxID: 543] |
Protein attributes
| Sequence length | 185 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 By similarity. |
| 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. |
| Sequence similarities | Belongs to the glycosyl hydrolase 24 family. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase |
| Technical term | 3D-structure |
| 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 – 185 | 185 | Lysozyme | PRO_0000218099 | ||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||
| Active site | 42 | 1 | Proton donor By similarity | |||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||
| Helix | 15 – 25 | 11 | ||||||||||||||||||||||||||||||||||||
| Helix | 32 – 38 | 7 | ||||||||||||||||||||||||||||||||||||
| Helix | 41 – 46 | 6 | ||||||||||||||||||||||||||||||||||||
| Helix | 48 – 50 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 53 – 55 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 74 – 95 | 22 | ||||||||||||||||||||||||||||||||||||
| Helix | 98 – 100 | 3 | ||||||||||||||||||||||||||||||||||||
| Helix | 103 – 116 | 14 | ||||||||||||||||||||||||||||||||||||
| Helix | 118 – 122 | 5 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 123 – 126 | 4 | ||||||||||||||||||||||||||||||||||||
| Turn | 127 – 130 | 4 | ||||||||||||||||||||||||||||||||||||
| Beta strand | 131 – 134 | 4 | ||||||||||||||||||||||||||||||||||||
| Helix | 136 – 142 | 7 | ||||||||||||||||||||||||||||||||||||
| Helix | 146 – 151 | 6 | ||||||||||||||||||||||||||||||||||||
| Helix | 152 – 155 | 4 | ||||||||||||||||||||||||||||||||||||
| Helix | 165 – 179 | 15 | ||||||||||||||||||||||||||||||||||||
| Turn | 180 – 182 | 3 | ||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Three functions of bacteriophage P1 involved in cell lysis." Schmidt C., Velleman M., Arber W. J. Bacteriol. 178:1099-1104(1996) [PubMed: 8576044] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | Lehnherr H., Bendtsen J.D., Preuss F., Ilyina T.V. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Genome of bacteriophage P1." Lobocka M.B., Rose D.J., Plunkett G. III, Rusin M., Samojedny A., Lehnherr H., Yarmolinsky M.B., Blattner F.R. J. Bacteriol. 186:7032-7068(2004) [PubMed: 15489417] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| X87673 Genomic DNA. Translation: CAA61013.1. AF125376 Genomic DNA. Translation: AAD20630.1. AF234172 Genomic DNA. Translation: AAQ13989.1. | |||||||||||||||||||
| RefSeq | YP_006484.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||
Protein family/group databases | |||||||||||||||||||
| CAZy | GH24. Glycoside Hydrolase Family 24. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 2777454. | ||||||||||||||||||
| GenomeReviews | Gene locus 17 in contig AF234172_GR. | ||||||||||||||||||
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_BPP1 | ||||||||
| Accession | Primary (citable) accession number: Q37875 | ||||||||
| Entry history |
| ||||||||
| 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


