Q6G1A8 (LSPA_BARQU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 48.
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 | Bartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 283165 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella |
Protein attributes
| Sequence length | 167 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 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 MF_00161 |
| Pathway | Protein modification; lipoprotein biosynthesis (signal peptide cleavage). HAMAP MF_00161 |
| Subcellular location | Cell inner membrane; Multi-pass membrane protein By similarity HAMAP 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: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 167 | 167 | Lipoprotein signal peptidase HAMAP MF_00161 | PRO_1000058231 | |||||
Regions | |||||||||
| Transmembrane | 8 – 28 | 21 | Helical; Potential | ||||||
| Transmembrane | 61 – 81 | 21 | Helical; Potential | ||||||
| Transmembrane | 93 – 113 | 21 | Helical; Potential | ||||||
| Transmembrane | 126 – 146 | 21 | Helical; Potential | ||||||
Sites | |||||||||
| Active site | 108 | 1 | By similarity | ||||||
| Active site | 136 | 1 | By similarity | ||||||
Sequences
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References
| [1] | "The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Toulouse. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX897700 Genomic DNA. Translation: CAF25516.1. |
| RefSeq | YP_031739.1. NC_005955.1. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | A08.001. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2867202. |
| GenomeReviews | Gene locus BQ00090 in contig BX897700_GR. |
| KEGG | bqu:BQ00090. |
| NMPDR | fig|283165.1.peg.9. |
| PATRIC | 31951131. VBIBarQui58630_0009. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG724422. |
| OMA | WLWKNTE. |
| PhylomeDB | Q6G1A8. |
| ProtClustDB | PRK14795. |
Enzyme and pathway databases | |
| BioCyc | BQUI283165:BQ00090-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00161. LspA. [Tree] |
| InterPro | IPR001872. Peptidase_A8. [Graphical view] |
| KO | K03101. |
| 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_BARQU | ||||||||
| Accession | Primary (citable) accession number: Q6G1A8 | ||||||||
| 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