Q1CV80 (LSPA_HELPH) 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: Lipoprotein signal peptidase EC=3.4.23.36 Alternative name(s): Prolipoprotein signal peptidase Signal peptidase II Short name=SPase II | ||||
| Gene names |
| ||||
| Organism | Helicobacter pylori (strain HPAG1) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 357544 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › ![]() |
Protein attributes
| Sequence length | 157 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 – 157 | 157 | Lipoprotein signal peptidase HAMAP-Rule MF_00161 | PRO_0000289391 | |||||
Regions | |||||||||
| Transmembrane | 10 – 30 | 21 | Helical; Potential | ||||||
| Transmembrane | 38 – 58 | 21 | Helical; Potential | ||||||
| Transmembrane | 59 – 79 | 21 | Helical; Potential | ||||||
| Transmembrane | 84 – 104 | 21 | Helical; Potential | ||||||
| Transmembrane | 122 – 142 | 21 | Helical; Potential | ||||||
Sites | |||||||||
| Active site | 105 | 1 | By similarity | ||||||
| Active site | 131 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression." Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HPAG1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000241 Genomic DNA. Translation: ABF84142.1. |
| RefSeq | YP_626816.1. NC_008086.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 357544.HPAG1_0075. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABF84142; ABF84142; HPAG1_0075. |
| GeneID | 4099024. |
| KEGG | hpa:HPAG1_0075. |
| PATRIC | 20601448. VBIHelPyl56048_0078. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0597. |
| HOGENOM | HOG000096992. |
| KO | K03101. |
| OMA | FRYESLM. |
| ProtClustDB | PRK00376. |
Enzyme and pathway databases | |
| BioCyc | HPYL357544:GH1F-119-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_HELPH | ||||||||
| Accession | Primary (citable) accession number: Q1CV80 | ||||||||
| 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
