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Q824E2 (LSPA_CHLCV) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:CCA_00210
OrganismChlamydophila caviae [Complete proteome] [HAMAP]
Taxonomic identifier83557 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length165 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 – 165165Lipoprotein signal peptidase HAMAP MF_00161
PRO_0000178774

Regions

Transmembrane7 – 2923Helical; Potential
Transmembrane70 – 8920Helical; Potential
Transmembrane101 – 12323Helical; Potential
Transmembrane138 – 15821Helical; Potential

Sites

Active site1151 By similarity
Active site1421 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q824E2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 586BB6E654DFC3F8

FASTA16519,160
        10         20         30         40         50         60 
MSSRSRSTFL AISFFVLIDW VSKLAVLLYR GNLPDARPIL YQYSWGKLIF CICPTFNEGA 

        70         80         90        100        110        120 
AFGIFSKYKY FLFAIRIAII LGILAFLFLR KKRTSPSIRF SLILLCSGAI GNVGDILFYR 

       130        140        150        160 
HVVDFISIGF KRWYFPTFNF ADIFISLGTF IFVYKLYFPT KQKIK 

« Hide

References

[1]"Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G. expand/collapse author list , Rank R.G., Bavoil P.M., Fraser C.M.
Nucleic Acids Res. 31:2134-2147(2003) [PubMed: 12682364] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GPIC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015925 Genomic DNA. Translation: AAP04961.1.
RefSeqNP_829083.1. NC_003361.3.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSA08.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1217895.
GenomeReviewsGene locus CCA_00210 in contig AE015925_GR.
KEGGcca:CCA00210.
PATRIC20269442. VBIChlCav107360_0220.
TIGRCCA_00210.

Phylogenomic databases

HOGENOMHBG724422.
OMARHVVDFI.
ProtClustDBPRK00376.

Enzyme and pathway databases

BioCycCCAV227941:CCA_00210-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_CHLCV
AccessionPrimary (citable) accession number: Q824E2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 52 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