Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9K9V2 (LSPA_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. 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
Synonyms:lsp
Ordered Locus Names:BH2543
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This protein specifically catalyzes the removal of signal peptides from prolipoproteins. 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 – 156156Lipoprotein signal peptidase HAMAP MF_00161
PRO_0000178768

Regions

Topological domain11Cytoplasmic Potential
Transmembrane2 – 2221Helical; Potential
Topological domain23 – 5129Extracellular Potential
Transmembrane52 – 7221Helical; Potential
Topological domain73 – 8412Cytoplasmic Potential
Transmembrane85 – 10521Helical; Potential
Topological domain106 – 12318Extracellular Potential
Transmembrane124 – 14421Helical; Potential
Topological domain145 – 15612Cytoplasmic Potential

Sites

Active site1021 By similarity
Active site1291 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K9V2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3670F52A55327B04

FASTA15617,828
        10         20         30         40         50         60 
MIYYIVALVI ILLDQWTKWL VVRHMEIGES IPLLDSVLYL TSHRNKGAAF GILEGQMWLF 

        70         80         90        100        110        120 
YIITSIVVIG IVYYMEKEAK HDRVFATALA LILGGAIGNF IDRIFRGEVV DFVNTYIFTY 

       130        140        150 
NFPIFNVADS ALCVGVGILF LKMIRDERKA KKEKNA 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB06262.1.
PIRG83967.
RefSeqNP_243409.1. NC_002570.2.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSA08.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000051231; EBBACP00000049870; EBBACG00000051222.
GeneID891512.
GenomeReviewsGene locus BH2543 in contig BA000004_GR.
KEGGbha:BH2543.
NMPDRfig|272558.1.peg.2543.
PATRIC18942278. VBIBacHal18977_2652.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000001848.
HOGENOMHBG724422.
OMAIASEIHG.
PhylomeDBQ9K9V2.
ProtClustDBPRK00376.

Enzyme and pathway databases

BioCycBHAL272558:BH2543-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_BACHD
AccessionPrimary (citable) accession number: Q9K9V2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 73 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