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Q8K9Z3 (LSPA_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipoprotein signal peptidase

EC=3.4.23.36
Alternative name(s):
Prolipoprotein signal peptidase
Signal peptidase II
Short name=SPase II
Gene names
Name:lspA
Ordered Locus Names:BUsg_141
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Protein existenceInferred 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 componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionAspartyl protease
Hydrolase
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 156156Lipoprotein signal peptidase HAMAP-Rule MF_00161
PRO_0000178772

Regions

Transmembrane5 – 2723Helical; Potential
Transmembrane39 – 5820Helical; Potential
Transmembrane68 – 8518Helical; Potential
Transmembrane97 – 11923Helical; Potential
Transmembrane129 – 14921Helical; Potential

Sites

Active site1111 By similarity
Active site1381 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9Z3 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: E5A3D4682F286DC2

FASTA15618,748
        10         20         30         40         50         60 
MKRKYYWIYI NIIFFIITVD FYSKKWILNH LNIYEKQKVF FILNLFHVHN FGAAFSILSD 

        70         80         90        100        110        120 
QNGWQKYFLL IFSIIIILAI IKIMIKFKKK DKNKILSYSL ILAGAIGNLI DRINYGFVID 

       130        140        150 
FIDLHFKSWH FATFNIADFS IFIGMIMIIK KNYYNS 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67709.1.
RefSeqNP_660498.1. NC_004061.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg141.

Protein family/group databases

MEROPSA08.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67709; AAM67709; BUsg_141.
GeneID1005958.
KEGGbas:BUsg141.
PATRIC21247063. VBIBucAph100086_0145.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0597.
KOK03101.
OMASYVVDMI.
OrthoDBEOG6PGKBM.
ProtClustDBPRK00376.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-151-MONOMER.
UniPathwayUPA00665.

Family and domain databases

HAMAPMF_00161. LspA.
InterProIPR001872. Peptidase_A8.
[Graphical view]
PfamPF01252. Peptidase_A8. 1 hit.
[Graphical view]
PRINTSPR00781. LIPOSIGPTASE.
TIGRFAMsTIGR00077. lspA. 1 hit.
PROSITEPS00855. SPASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLSPA_BUCAP
AccessionPrimary (citable) accession number: Q8K9Z3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: February 19, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names