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Q0PBE9 (LSPA_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:Cj0361
OrganismCampylobacter jejuni
Taxonomic identifier197 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

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 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 componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionAspartyl protease
Hydrolase
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to 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-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 156156Lipoprotein signal peptidase HAMAP MF_00161
PRO_1000097243

Regions

Transmembrane5 – 2521Helical; Potential
Transmembrane39 – 5820Helical; Potential
Transmembrane64 – 8421Helical; Potential
Transmembrane89 – 10921Helical; Potential
Transmembrane122 – 14221Helical; Potential

Sites

Active site1041 By similarity
Active site1301 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0PBE9 [UniParc].

Last modified September 19, 2006. Version 1.
Checksum: DF2E6E4107F41733

FASTA15618,327
        10         20         30         40         50         60 
MAKTFKFIFY FWGAFVLVFA LDQWVKSLTL AGFRWQSEYL DLTYALNTGV AFSMLSFLEH 

        70         80         90        100        110        120 
NLKYLHLALI GVLFIYLFWQ RTLLKTHSIA FGMMLGAGVS NLLDRFIHGG VVDMFFWHKW 

       130        140        150 
FNFAIFNVAD VMINISVALI LIQEIFKKRK KDDRMD 

« Hide

References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed: 10688204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL111168 Genomic DNA. Translation: CAL34511.1.
PIRG81378.
RefSeqYP_002343798.1. NC_002163.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ0PBE9. 7 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID904684.
GenomeReviewsGene locus Cj0361 in contig AL111168_GR.
KEGGcje:Cj0361.
PATRIC20057637. VBICamJej33762_0352.

Phylogenomic databases

HOGENOMHBG724422.
OMAGVAFSMF.
ProtClustDBPRK00376.

Enzyme and pathway databases

BioCycCJEJ192222:CJ0361-MONOMER.

Family and domain databases

HAMAPMF_00161. LspA.
[Tree]
InterProIPR001872. Peptidase_A8.
[Graphical view]
KOK03101.
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_CAMJE
AccessionPrimary (citable) accession number: Q0PBE9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 19, 2006
Last modified: January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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