Reviewed,
UniProtKB/Swiss-Prot O32041 (YRVJ_BACSU)
Last modified
November 3, 2009.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative N-acetylmuramoyl-L-alanine amidase yrvJ EC=3.5.1.28 | ||||
| Gene names |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 518 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 | Probably involved in cell-wall metabolism By similarity. |
| Catalytic activity | Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. |
| Subcellular location | |
| Sequence similarities | Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell wall biogenesis/degradation |
| Cellular component | Cell wall Secreted |
| Domain | Signal |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic processInferred from electronic annotation. Source: InterPro |
| Cellular component | cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular regionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: EC zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| AL009126 Genomic DNA. Translation: CAB14717.1. | |
| PIR | B69981. |
| RefSeq | NP_390636.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NQM based on UniProtKB P22629. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 937544. |
| GenomeReviews | Gene locus BSU27580 in contig AL009126_GR. |
| KEGG | bsu:BSU27580. |
| NMPDR | fig|224308.1.peg.2761. |
Organism-specific databases | |
| SubtiList | BG13806. yrvJ. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O32041. |
| OMA | YVANWVV. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU2754-MON. |
Family and domain databases | |
| InterPro | IPR002508. CW_Hdrlase/autolysin_cat. IPR017293. N-acetylmuramoyl-L-ala_amidase. IPR013247. SH3_3. IPR003646. SH3_bac. [Graphical view] |
| Gene3D | G3DSA:3.40.630.40. Cell_wall_OHase/autolysin_cat. 1 hit. |
| Pfam | PF01520. Amidase_3. 1 hit. PF08239. SH3_3. 4 hits. [Graphical view] |
| PIRSF | PIRSF037846. Autolysin_YrvJ_prd. 1 hit. |
| SMART | SM00646. Ami_3. 1 hit. SM00287. SH3b. 4 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | YRVJ_BACSU | ||||||||
| Accession | Primary (citable) accession number: O32041 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

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