P10335 (LIP2_STAAU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 72.
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: Lipase 2 EC=3.1.1.3 Alternative name(s): Glycerol ester hydrolase 2 | ||||
| Gene names |
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| Organism | Staphylococcus aureus | ||||
| Taxonomic identifier | 1280 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 690 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | Triacylglycerol + H2O = diacylglycerol + a carboxylate. |
| Subcellular location | |
| Miscellaneous | The expression of Staphylococcus lipase is negatively regulated by bacteriophage lysogenization (lipase conversion). |
| Sequence similarities | Belongs to the AB hydrolase superfamily. Lipase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase |
| PTM | Zymogen |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membraneInferred from electronic annotation. Source: InterPro |
| Molecular function | triglyceride lipase 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 37 | 37 | Potential | ||||||
| Propeptide | 38 – 295 | 258 | PRO_0000017752 | ||||||
| Chain | 296 – 690 | 395 | Lipase 2 | PRO_0000017753 | |||||
Regions | |||||||||
| Region | 311 – 690 | 380 | Hydrophobic | ||||||
Sites | |||||||||
| Active site | 412 | 1 | Charge relay system By similarity | ||||||
| Active site | 645 | 1 | Charge relay system By similarity | ||||||
Sequences
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References
| [1] | "Lysogenic conversion of staphylococcal lipase is caused by insertion of the bacteriophage L54a genome into the lipase structural gene." Lee C.Y., Iandolo J.J. J. Bacteriol. 166:385-391(1986) [PubMed: 3009394] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "In vivo processing of Staphylococcus aureus lipase." Rollof J., Normark S. J. Bacteriol. 174:1844-1847(1992) [PubMed: 1548232] [Abstract] Cited for: PROTEIN SEQUENCE OF 296-307, PROTEOLYTIC PROCESSING. Strain: TEN 5. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M12715 Genomic DNA. Translation: AAA26633.1. |
| PIR | A24545. |
3D structure databases | |
| ProteinModelPortal | P10335. |
| SMR | P10335. Positions 295-682. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR005877. Gpos_YSIRK. [Graphical view] |
| Pfam | PF04650. YSIRK_signal. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01168. YSIRK_signal. 1 hit. |
| PROSITE | PS00120. LIPASE_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LIP2_STAAU | ||||||||
| Accession | Primary (citable) accession number: P10335 | ||||||||
| 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 |

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