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Q5P9U0 (LSPA_ANAMM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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:AM1081
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length170 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 – 170170Lipoprotein signal peptidase HAMAP MF_00161
PRO_1000076914

Regions

Transmembrane5 – 2521Helical; Potential
Transmembrane62 – 8221Helical; Potential
Transmembrane89 – 11123Helical; Potential
Transmembrane126 – 14621Helical; Potential

Sites

Active site1061 By similarity
Active site1331 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5P9U0 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: A7DA88C94C9D0743

FASTA17018,587
        10         20         30         40         50         60 
MKSKIVGVIA IVLVFALDQV SKAYAIDWYS QSGATEIFKF CSLVEVWNRG ISFGMFGALE 

        70         80         90        100        110        120 
SSNLIFTYVS LGVILMLFVL FVQSKCNKST ICMGVVIGGA LGNLADRLRF GAVYDFVSLH 

       130        140        150        160        170 
AGEFHWPAFN FADVCVTCGV ICFLCLEIMY HAKACVDTSG DPDALSVKKY 

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References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: St. Maries.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000030 Genomic DNA. Translation: AAV86940.1.
RefSeqYP_154195.1. NC_004842.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5P9U0.

Protein family/group databases

MEROPSA08.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3170986.
GenomeReviewsGene locus AM1081 in contig CP000030_GR.
KEGGama:AM1081.
PATRIC20948055. VBIAnaMar46146_0940.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0597.
HOGENOMHBG724422.
OMAWLARVEY.
ProtClustDBPRK14775.

Enzyme and pathway databases

BioCycAMAR234826:AM1081-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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLSPA_ANAMM
AccessionPrimary (citable) accession number: Q5P9U0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 46 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