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P75484 (LSPA_MYCPN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Synonyms:lsp
Ordered Locus Names:MPN_293
ORF Names:MP542
OrganismMycoplasma pneumoniae (strain ATCC 29342 / M129) [Reference proteome] [HAMAP]
Taxonomic identifier272634 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   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...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MPN_387P753951EBI-2258812,EBI-2258802

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 184184Lipoprotein signal peptidase HAMAP-Rule MF_00161
PRO_0000178795

Regions

Transmembrane23 – 4321Helical; Potential
Transmembrane88 – 10821Helical; Potential
Transmembrane110 – 13021Helical; Potential
Transmembrane156 – 17621Helical; Potential

Sites

Active site1311 By similarity
Active site1571 By similarity

Sequences

Sequence LengthMass (Da)Tools
P75484 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: C29480B17C7B98A3

FASTA18420,586
        10         20         30         40         50         60 
MAKAPTFFSK LLKQILFANR KPFLYYKLAL ILFVGFVILF QVFMLRAALN GEKGINGANG 

        70         80         90        100        110        120 
TDVARSSFIS IYVIGNKGVG FSLLADQPGL VYFLQGFLSF IALFFLVFST SYNYIFWITT 

       130        140        150        160        170        180 
LAFGSLGNFF DRLTSGSGEV LDYFVFSGGN SVFNLADCCI TFSFIGLFLS FLIQFFKEMK 


QTKS 

« Hide

References

[1]"Complete sequence analysis of the genome of the bacterium Mycoplasma pneumoniae."
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.
Nucleic Acids Res. 24:4420-4449(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29342 / M129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00089 Genomic DNA. Translation: AAB96190.1.
PIRS73868.
RefSeqNP_109981.1. NC_000912.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP75484. 1 interaction.
STRING272634.MPN293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB96190; AAB96190; MPN_293.
GeneID877085.
KEGGmpn:MPN293.
PATRIC20021921. VBIMycPne110_0317.

Phylogenomic databases

eggNOGCOG0597.
KOK03101.
OMAYIFWITT.
OrthoDBEOG647V1T.
ProtClustDBPRK00573.

Enzyme and pathway databases

BioCycMPNE272634:GJ6Z-300-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_MYCPN
AccessionPrimary (citable) accession number: P75484
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: February 19, 2014
This is version 91 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

Mycoplasma pneumoniae

Mycoplasma pneumoniae (strain M129): entries and gene names