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A7H513 (LSPA_CAMJD) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:JJD26997_1596
OrganismCampylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97) [Complete proteome] [HAMAP]
Taxonomic identifier360109 [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
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_1000097242

Regions

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

Sites

Active site1041 By similarity
Active site1301 By similarity

Sequences

Sequence LengthMass (Da)Tools
A7H513 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 0B7BE3F1BBC30CBB

FASTA15618,290
        10         20         30         40         50         60 
MAKTFKFIFY FWGAFVLVFA LDQWVKSLTL AGLRWQSKYL DLTYALNTGV AFSMLSFLEH 

        70         80         90        100        110        120 
NLKYLHLALI GVLFIYLFWQ KTLLKTHSIA FGMMLGAGVS NLLDRFIYGG VVDMFFWHKW 

       130        140        150 
FNFAIFNVAD VMINISVALI LIQEIFKKRK KDDRMD 

« Hide

References

[1]"Complete genome sequence of Campylobacter jejuni subsp doylei 269.97 isolated from human blood."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1458 / RM4099 / 269.97.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000768 Genomic DNA. Translation: ABS43452.1.
RefSeqYP_001398593.1. NC_009707.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7H513.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5389512.
GenomeReviewsGene locus JJD26997_1596 in contig CP000768_GR.
KEGGcjd:JJD26997_1596.
PATRIC20048864. VBICamJej122183_1576.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0597.
HOGENOMHBG724422.
OMAGVAFSMF.
ProtClustDBPRK00376.

Enzyme and pathway databases

BioCycCJEJ360109:JJD26997_1596-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_CAMJD
AccessionPrimary (citable) accession number: A7H513
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 11, 2007
Last modified: December 14, 2011
This is version 36 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