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Reviewed, UniProtKB/Swiss-Prot Q6G1A8 (LSPA_BARQU)

Last modified February 9, 2010. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: BQ00090
OrganismBartonella quintana (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier803 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length167 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
   Molecular functionAspartyl protease
Hydrolase
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: HAMAP

   Molecular functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 167167Lipoprotein signal peptidase HAMAP MF_00161
PRO_1000058231

Regions

Transmembrane8 – 2821 Potential
Transmembrane61 – 8121 Potential
Transmembrane93 – 11321 Potential
Transmembrane126 – 14621 Potential

Sites

Active site1081 By similarity
Active site1361 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6G1A8-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: A5EBE14A54160ABF

FASTA16719,631
        10         20         30         40         50         60 
MTRKSFSFFL LGLILTVGID QTVKYWIMHN MLLGTEIPLL PFLSLYHVRN SGIAFSFFSS 

        70         80         90        100        110        120 
FSHWGLIALT LIILIFLLWL WKNTEYNKFL SRFGLTLIIG GAIGNLIDRI CFYYVIDYIL 

       130        140        150        160 
FYIDDIFYFA VFNLADTFIT LGVIAIVTEE LRIWIKEKRH SKRTFSR 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897700 Genomic DNA. Translation: CAF25516.1.
RefSeqYP_031739.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSA08.001.

Genome annotation databases

GeneID2867202.
GenomeReviewsGene locus BQ00090 in contig BX897700_GR.
KEGGbqu:BQ00090.
NMPDRfig|283165.1.peg.9.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG724422.
OMAAHPGQKL.
PhylomeDBQ6G1A8.

Enzyme and pathway databases

BioCycBQUI283165:BQ00090-MONOMER.
BRENDA3.4.23.36. 292235.

Family and domain databases

HAMAPMF_00161. LspA.
[Tree]
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_BARQU
AccessionPrimary (citable) accession number: Q6G1A8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 19, 2004
Last modified: February 9, 2010
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents