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C3PND1 (LSPA_RICAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 33. 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:RAF_ORF0520
OrganismRickettsia africae (strain ESF-5) [Complete proteome] [HAMAP]
Taxonomic identifier347255 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length201 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)
   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 – 201201Lipoprotein signal peptidase HAMAP-Rule MF_00161
PRO_1000203595

Regions

Transmembrane73 – 9321Helical; Potential
Transmembrane97 – 11721Helical; Potential
Transmembrane135 – 15521Helical; Potential

Sites

Active site1171 By similarity
Active site1441 By similarity

Sequences

Sequence LengthMass (Da)Tools
C3PND1 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 00A080A03DA9139D

FASTA20123,483
        10         20         30         40         50         60 
MLPLLKKLYL TFARSSRIII TLVIIDQLSK WWFIDNLRWK PDLMLKFTSF LNMVYTWNYG 

        70         80         90        100        110        120 
ISFGLMREYY QYSNAIFLIT NTIIVCYLYY LMIRSKTIGS FAGYSFVIGG AVGNLIDRFF 

       130        140        150        160        170        180 
RGAVFDFIHF HYQNYSFPVF NLADCFITIG VIILIEDYYS TKKVIEEKAK GNYDNAQIEA 

       190        200 
MAEKIRNTDK GGNDKIASLQ N 

« Hide

References

[1]"Analysis of the Rickettsia africae genome reveals that virulence acquisition in Rickettsia species may be explained by genome reduction."
Fournier P.-E., El Karkouri K., Leroy Q., Robert C., Giumelli B., Renesto P., Socolovschi C., Parola P., Audic S., Raoult D.
BMC Genomics 10:166-166(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ESF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001612 Genomic DNA. Translation: ACP53441.1.
RefSeqYP_002845184.1. NC_012633.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING347255.RAF_ORF0520.

Protein family/group databases

MEROPSA08.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP53441; ACP53441; RAF_ORF0520.
GeneID7814944.
KEGGraf:RAF_ORF0520.
PATRIC17872982. VBIRicAfr6986_0626.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0597.
HOGENOMHOG000096992.
KOK03101.
OMAGNTEHRT.
OrthoDBEOG6PGKBM.

Enzyme and pathway databases

BioCycRAFR347255:GJCT-492-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_RICAE
AccessionPrimary (citable) accession number: C3PND1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: May 14, 2014
This is version 33 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