Q0SN37 (LSPA_BORAP) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 52.
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 |
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| Organism | Borrelia afzelii (strain PKo) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 390236 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group › ![]() |
Protein attributes
| Sequence length | 170 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 inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_00161. |
| Sequence similarities | Belongs to the peptidase A8 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell inner membrane 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 – 170 | 170 | Lipoprotein signal peptidase HAMAP-Rule MF_00161 | PRO_0000289355 | |||||
Regions | |||||||||
| Transmembrane | 9 – 29 | 21 | Helical; Potential | ||||||
| Transmembrane | 72 – 92 | 21 | Helical; Potential | ||||||
| Transmembrane | 96 – 118 | 23 | Helical; Potential | ||||||
| Transmembrane | 143 – 163 | 21 | Helical; Potential | ||||||
Sites | |||||||||
| Active site | 114 | 1 | By similarity | ||||||
| Active site | 146 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity." Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J., Wilske B., Platzer M. BMC Genomics 7:211-211(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PKo. |
| [2] | "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii Lyme disease agent isolates." Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J., Fraser-Liggett C.M., Schutzer S.E. J. Bacteriol. 193:6995-6996(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PKo. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000395 Genomic DNA. Translation: ABH01741.1. CP002933 Genomic DNA. Translation: AEL69695.1. |
| RefSeq | YP_005592685.1. NC_017238.1. YP_709917.1. NC_008277.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 390236.BAPKO_0498. |
Protein family/group databases | |
| MEROPS | A08.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABH01741; ABH01741; BAPKO_0498. AEL69695; AEL69695; BafPKo_0487. |
| GeneID | 12159435. 4227949. |
| KEGG | baf:BAPKO_0498. bafz:BafPKo_0487. |
| PATRIC | 37189271. VBIBorAfz3878_0535. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0597. |
| HOGENOM | HOG000096992. |
| KO | K03101. |
| OMA | KYLVVKY. |
| ProtClustDB | PRK01574. |
Enzyme and pathway databases | |
| 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_BORAP | ||||||||
| Accession | Primary (citable) accession number: Q0SN37 Secondary accession number(s): G0ISB4 | ||||||||
| 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
