C1NGQ4 (C1NGQ4_9ESCH) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 11.
History...
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Lysozyme RuleBase RU003788 EC=3.2.1.17 RuleBase RU003788 | ||
| Gene names |
| ||
| Organism | Escherichia sp. 1_1_43 EMBL EEH70617.1 | ||
| Taxonomic identifier | 457400 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 165 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| 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. RuleBase RU003788 |
| Sequence similarities | Belongs to the glycosyl hydrolase 24 family. RuleBase RU003788 |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Antimicrobial Bacteriolytic enzyme RuleBase RU003788 Glycosidase RuleBase RU003788 Hydrolase |
| 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... | |
Sequences
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References
| [1] | "The Genome Sequence of Escherichia sp. strain 1_1_43." The Broad Institute Genome Sequencing Platform Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C. Birren B.Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: 1_1_43 EMBL EEH70617.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | GG665838 Genomic DNA. Translation: EEH70617.1. |
3D structure databases | |
| ProteinModelPortal | C1NGQ4. |
| SMR | C1NGQ4. Positions 7-164. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| PATRIC | 31135432. VBIEscSp5885_1999. |
Family and domain databases | |
| InterPro | IPR002196. Glyco_hydro_24. IPR023346. Lysozyme-like_dom. [Graphical view] |
| Pfam | PF00959. Phage_lysozyme. 1 hit. [Graphical view] |
| SUPFAM | SSF53955. SSF53955. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | C1NGQ4_9ESCH | ||||||||
| Accession | Primary (citable) accession number: C1NGQ4 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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