C3PND1 (LSPA_RICAE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 29.
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: Lipoprotein signal peptidase EC=3.4.23.36 Alternative name(s): Prolipoprotein signal peptidase Signal peptidase II Short name=SPase II | ||||
| Gene names |
| ||||
| Organism | Rickettsia africae (strain ESF-5) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 347255 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group › ![]() |
Protein attributes
| Sequence length | 201 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | This protein specifically catalyzes the removal of signal peptides from prolipoproteins By similarity. HAMAP-Rule MF_00161 |
| Catalytic activity | Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains. HAMAP-Rule MF_00161 |
| Pathway | Protein modification; lipoprotein biosynthesis (signal peptide cleavage). HAMAP-Rule MF_00161 |
| Subcellular location | Cell membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_00161. |
| Sequence similarities | Belongs to the peptidase A8 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Molecular function | Aspartyl protease Hydrolase Protease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | aspartic-type endopeptidase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 201 | 201 | Lipoprotein signal peptidase HAMAP-Rule MF_00161 | PRO_1000203595 | |||||
Regions | |||||||||
| Transmembrane | 73 – 93 | 21 | Helical; Potential | ||||||
| Transmembrane | 97 – 117 | 21 | Helical; Potential | ||||||
| Transmembrane | 135 – 155 | 21 | Helical; Potential | ||||||
Sites | |||||||||
| Active site | 117 | 1 | By similarity | ||||||
| Active site | 144 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "Analysis of the Rickettsia africae genome reveals that virulence acquisition in Rickettsia species may be explained by genome reduction." Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B., Renesto P., Socolovschi C., Parola P., Audic S., Raoult D. BMC Genomics 10:166-166(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ESF-5. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001612 Genomic DNA. Translation: ACP53441.1. |
| RefSeq | YP_002845184.1. NC_012633.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 347255.RAF_ORF0520. |
Protein family/group databases | |
| MEROPS | A08.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ACP53441; ACP53441; RAF_ORF0520. |
| GeneID | 7814944. |
| KEGG | raf:RAF_ORF0520. |
| PATRIC | 17872982. VBIRicAfr6986_0626. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0597. |
| HOGENOM | HOG000096992. |
| KO | K03101. |
| OMA | ICSKTIG. |
| ProtClustDB | PRK00376. |
Enzyme and pathway databases | |
| BioCyc | RAFR347255:GJCT-492-MONOMER. |
| UniPathway | UPA00665. |
Family and domain databases | |
| HAMAP | MF_00161. LspA. |
| InterPro | IPR001872. Peptidase_A8. [Graphical view] |
| Pfam | PF01252. Peptidase_A8. 1 hit. [Graphical view] |
| PRINTS | PR00781. LIPOSIGPTASE. |
| TIGRFAMs | TIGR00077. lspA. 1 hit. |
| PROSITE | PS00855. SPASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LSPA_RICAE | ||||||||
| Accession | Primary (citable) accession number: C3PND1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
