Q4L3C1 (SLE1_STAHJ) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 51.
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 sle1 EC=3.5.1.28 | ||||||
| Gene names |
| ||||||
| Organism | Staphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 279808 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 329 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 | Peptidoglycan hydrolase involved in the splitting of the septum during cell division By similarity. |
| Catalytic activity | Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. |
| Subcellular location | Secreted By similarity. Cell surface By similarity. |
| Sequence similarities | Contains 3 LysM repeats. Contains 1 peptidase C51 domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 26 | 26 | Potential | ||||||
| Chain | 27 – 329 | 303 | N-acetylmuramoyl-L-alanine amidase sle1 | PRO_0000231629 | |||||
Regions | |||||||||
| Repeat | 30 – 72 | 43 | LysM 1 | ||||||
| Repeat | 90 – 132 | 43 | LysM 2 | ||||||
| Repeat | 154 – 196 | 43 | LysM 3 | ||||||
| Domain | 205 – 329 | 125 | Peptidase C51 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species." Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K. J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCSC1435. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AP006716 Genomic DNA. Translation: BAE05856.1. |
| RefSeq | YP_254462.1. NC_007168.1. |
3D structure databases | |
| ProteinModelPortal | Q4L3C1. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAE05856; BAE05856; SH2547. |
| GeneID | 3482633. |
| KEGG | sha:SH2547. |
| PATRIC | 19621195. VBIStaHae67511_2500. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG3942. |
| HOGENOM | HOG000279823. |
| OMA | LIASKYN. |
| ProtClustDB | CLSK884669. |
Enzyme and pathway databases | |
| BioCyc | SHAE279808:GJX7-2622-MONOMER. |
Family and domain databases | |
| InterPro | IPR007921. CHAP. IPR018392. Peptidoglycan-bd_lysin. IPR002482. Peptidoglycan-bd_Lysin_subgr. [Graphical view] |
| Pfam | PF05257. CHAP. 1 hit. PF01476. LysM. 3 hits. [Graphical view] |
| SMART | SM00257. LysM. 3 hits. [Graphical view] |
| PROSITE | PS50911. CHAP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SLE1_STAHJ | ||||||||
| Accession | Primary (citable) accession number: Q4L3C1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
