Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q71YH2 (LSPA_LISMF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:LMOf2365_1872
OrganismListeria monocytogenes serotype 4b (strain F2365) [Complete proteome] [HAMAP]
Taxonomic identifier265669 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length154 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 – 154154Lipoprotein signal peptidase HAMAP-Rule MF_00161
PRO_0000178792

Regions

Transmembrane56 – 7520Helical; Potential
Transmembrane84 – 10623Helical; Potential
Transmembrane121 – 14323Helical; Potential

Sites

Active site1021 By similarity
Active site1291 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q71YH2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 78A786C13071ED37

FASTA15417,707
        10         20         30         40         50         60 
MYYYLITLAV IALDQLTKWI VVQNMEIGQK IEVIPGFLYW TSYRNDGAAW SILEGHMWFF 

        70         80         90        100        110        120 
YLITVVVIGI IIYIMQKYAK GKRLFSISLA FILGGAIGNF IDRVLHQEVV DFVQTVWGNY 

       130        140        150 
YFPIFNVADA ALSVGVVLML VYVFVDDRKT KGIK 

« Hide

References

[1]"Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne pathogen Listeria monocytogenes reveal new insights into the core genome components of this species."
Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M., Daugherty S.C., Dodson R.J. expand/collapse author list , Durkin A.S., Madupu R., Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O., Luchansky J.B., Fraser C.M.
Nucleic Acids Res. 32:2386-2395(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: F2365.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017262 Genomic DNA. Translation: AAT04642.1.
RefSeqYP_014465.1. NC_002973.6.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING265669.LMOf2365_1872.

Protein family/group databases

MEROPSA08.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT04642; AAT04642; LMOf2365_1872.
GeneID2799113.
KEGGlmf:LMOf2365_1872.
PATRIC20325037. VBILisMon105049_1878.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0597.
HOGENOMHOG000096992.
KOK03101.
OMADFASKQW.
OrthoDBEOG6PGKBM.

Enzyme and pathway databases

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_LISMF
AccessionPrimary (citable) accession number: Q71YH2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 70 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