P14892 (CWLA_BACSP) 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: N-acetylmuramoyl-L-alanine amidase CwlA EC=3.5.1.28 Alternative name(s): Autolysin Cell wall hydrolase | ||
| Gene names |
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| Organism | Bacillus sp. | ||
| Taxonomic identifier | 1409 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus![]() |
Protein attributes
| Sequence length | 251 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation. |
| Catalytic activity | Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. |
| Subcellular location | Secreted Potential. |
| Miscellaneous | Retention of enzymatic activity was limited to the N-terminal fragment (AA 1-196). |
| Sequence similarities | Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell wall biogenesis/degradation Competence Sporulation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Antimicrobial Bacteriolytic enzyme Hydrolase |
| Gene Ontology (GO) | |
| Biological_process | cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW establishment of competence for transformationInferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic processInferred from electronic annotation. Source: InterPro sporulation resulting in formation of a cellular sporeInferred from electronic annotation. Source: UniProtKB-KW |
| 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)
Sequences
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References
| [1] | "Cloning, sequencing and expression of a Bacillus bacteriolytic enzyme in Escherichia coli." Potvin C., Leclerc D., Tremblay G., Asselin A., Bellemare G. Mol. Gen. Genet. 214:241-248(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X13524 Genomic DNA. Translation: CAA31877.1. |
| PIR | S08306. |
3D structure databases | |
| ProteinModelPortal | P14892. |
| SMR | P14892. Positions 1-147. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.40.80.10. 1 hit. |
| InterPro | IPR021976. Amidase02_C. IPR002502. Amidase_domain. [Graphical view] |
| Pfam | PF12123. Amidase02_C. 1 hit. PF01510. Amidase_2. 1 hit. [Graphical view] |
| SMART | SM00644. Ami_2. 1 hit. [Graphical view] |
| SUPFAM | SSF55846. Amidase_2. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | CWLA_BACSP | ||||||||
| Accession | Primary (citable) accession number: P14892 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
