P32762 (ALYS_BPHB3) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 64.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Lytic amidase EC=3.5.1.28 Alternative name(s): N-acetylmuramoyl-L-alanine amidase | ||
| Gene names |
| ||
| Organism | Streptococcus pneumoniae phage HB-3 | ||
| Taxonomic identifier | 10728 [NCBI] | ||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Caudovirales › Siphoviridae › ![]() | ||
| Virus host | Streptococcus pneumoniae [TaxID: 1313] |
Protein attributes
| Sequence length | 318 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. |
| Subcellular location | Secreted Potential. |
| Sequence similarities | Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. Contains 6 cell wall-binding repeats. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell wall biogenesis/degradation |
| Cellular component | Secreted |
| Domain | Repeat |
| Molecular function | Antimicrobial Bacteriolytic enzyme Hydrolase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic processInferred from electronic annotation. Source: InterPro |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | N-acetylmuramoyl-L-alanine amidase 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 – 318 | 318 | Lytic amidase | PRO_0000164406 | |||||
Regions | |||||||||
| Repeat | 175 – 194 | 20 | Cell wall-binding 1 | ||||||
| Repeat | 196 – 215 | 20 | Cell wall-binding 2 | ||||||
| Repeat | 217 – 237 | 21 | Cell wall-binding 3 | ||||||
| Repeat | 238 – 257 | 20 | Cell wall-binding 4 | ||||||
| Repeat | 258 – 277 | 20 | Cell wall-binding 5 | ||||||
| Repeat | 280 – 301 | 22 | Cell wall-binding 6 | ||||||
Sequences
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References
| [1] | "Sequence of the Streptococcus pneumoniae bacteriophage HB-3 amidase reveals high homology with the major host autolysin." Romero A., Lopez R., Garcia P. J. Bacteriol. 172:5064-5070(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Characterization of the pneumococcal bacteriophage HB-3 amidase: cloning and expression in Escherichia coli." Romero A., Lopez R., Garcia P. J. Virol. 64:137-142(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M34652 Genomic DNA. Translation: AAA50574.1. |
| PIR | S16016. |
3D structure databases | |
| ProteinModelPortal | P32762. |
| SMR | P32762. Positions 188-318. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR002502. Amidase_domain. IPR018337. Cell_wall/Cho-bd_repeat. [Graphical view] |
| Pfam | PF01510. Amidase_2. 1 hit. PF01473. CW_binding_1. 5 hits. [Graphical view] |
| SMART | SM00644. Ami_2. 1 hit. [Graphical view] |
| SUPFAM | SSF55846. Amidase_2. 1 hit. |
| PROSITE | PS51170. CW. 6 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ALYS_BPHB3 | ||||||||
| Accession | Primary (citable) accession number: P32762 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
