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A7GRL8 (LSPA_BACCN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 39. 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:Bcer98_2542
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length152 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 membrane; Multi-pass membrane protein By similarity HAMAP 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)
   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 – 152152Lipoprotein signal peptidase HAMAP MF_00161
PRO_1000190792

Regions

Transmembrane55 – 7521Helical; Potential
Transmembrane85 – 10521Helical; Potential
Transmembrane124 – 14421Helical; Potential

Sites

Active site1021 By similarity
Active site1291 By similarity

Sequences

Sequence LengthMass (Da)Tools
A7GRL8 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 53287E1010A93E42

FASTA15217,460
        10         20         30         40         50         60 
MIYYLIALFV IAIDQLSKWF IVKNMELGAS IPIIDNVLYI TSHRNRGAAW GILENKMWFF 

        70         80         90        100        110        120 
YIITVVFVGF IVFYMKKYAK TDKLLGISLG LILGGAIGNF IDRVFRQEVV DFIHVYIFSY 

       130        140        150 
NYPVFNIADS ALCIGVVLII IQTLLEGKKM KE 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NVH 391-98.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000764 Genomic DNA. Translation: ABS22776.1.
RefSeqYP_001375771.1. NC_009674.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA7GRL8.

Protein family/group databases

MEROPSA08.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000038646; EBBACP00000037697; EBBACG00000038637.
GeneID5344022.
GenomeReviewsGene locus Bcer98_2542 in contig CP000764_GR.
KEGGbcy:Bcer98_2542.
PATRIC18933682. VBIBacCyt128034_2685.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0597.
GeneTreeEBGT00050000001848.
HOGENOMHBG724422.
OMAIASEIHG.
ProtClustDBPRK00376.

Enzyme and pathway databases

BioCycBCER315749:BCER98_2542-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_BACCN
AccessionPrimary (citable) accession number: A7GRL8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 11, 2007
Last modified: December 14, 2011
This is version 39 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