Reviewed,
UniProtKB/Swiss-Prot Q8CPQ1 (ATL_STAES)
Last modified
January 19, 2010.
Version 43.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Bifunctional autolysin Including the following 2 domains: 1- Recommended name: N-acetylmuramoyl-L-alanine amidase EC=3.5.1.28 2- Recommended name: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC=3.2.1.96 | ||||
| Gene names |
| ||||
| Organism | Staphylococcus epidermidis (strain ATCC 12228) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 176280 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 1335 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 | Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis By similarity. |
| Catalytic activity | Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)2)Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. |
| Subunit structure | Oligomer; forms a ring structure at the cell surface which is important for efficient partitioning of daughter cells after cell division By similarity. |
| Subcellular location | Secreted By similarity. Note: Secreted, and then anchored on the cell surface at the peripheral cell wall above the completed septum (septal region), for the next cell division cycle By similarity. |
| Domain | The repeat domains R1, R2 and R3 are responsible for directing the proteins to the septal region By similarity. |
| Post-translational modification | Undergoes proteolytic processing to generate the two extracellular lytic enzymes, probably at the septal region on the cell surface By similarity. |
| Sequence similarities | In the N-terminal section; belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. In the C-terminal section; belongs to the glycosyl hydrolase 73 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell wall biogenesis/degradation |
| Cellular component | Secreted |
| Domain | Repeat Signal |
| Molecular function | Hydrolase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | cellular cell wall macromolecule metabolic process Inferred from electronic annotation. Source: InterPro cellular cell wall organizationInferred 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 amidase activityInferred from electronic annotation. Source: InterPro mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 29 | 29 | Potential | ||||||
| Chain | 30 – 1335 | 1306 | Bifunctional autolysin | PRO_0000045481 | |||||
Regions | |||||||||
| Repeat | 516 – 681 | 166 | 1 | ||||||
| Repeat | 682 – 845 | 164 | 2 | ||||||
| Repeat | 846 – 1015 | 170 | 3 | ||||||
| Region | 303 – 863 | 561 | N-acetylmuramoyl-L-alanine amidase | ||||||
| Region | 864 – 1335 | 472 | Endo-beta-N-acetylglucosaminidase | ||||||
Sequences
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References
| [1] | "Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)." Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M. Mol. Microbiol. 49:1577-1593(2003) [PubMed: 12950922] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE015929 Genomic DNA. Translation: AAO04347.1. |
| RefSeq | NP_764305.1. |
3D structure databases | |
| SMR | Q8CPQ1. Positions 347-488. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q8CPQ1. |
Protein family/group databases | |
| CAZy | GH73. Glycoside Hydrolase Family 73. |
Genome annotation databases | |
| GeneID | 1055684. |
| GenomeReviews | Gene locus SE_0750 in contig AE015929_GR. |
| KEGG | sep:SE0750. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG5632. |
| HOGENOM | HBG692910. |
| OMA | KSGWISK. |
Enzyme and pathway databases | |
| BioCyc | SEPI176280:SE_0750-MONOMER. |
Family and domain databases | |
| InterPro | IPR002502. Amidase_2. IPR013338. Lysozyme_dom_subfam2. IPR002901. Mano_Glyc_endo_b_GlcNAc. [Graphical view] |
| Pfam | PF01510. Amidase_2. 1 hit. PF01832. Glucosaminidase. 1 hit. [Graphical view] |
| SMART | SM00644. Ami_2. 1 hit. SM00047. LYZ2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ATL_STAES | ||||||||
| Accession | Primary (citable) accession number: Q8CPQ1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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