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Reviewed, UniProtKB/Swiss-Prot Q45479 (LSPA_BACSU)

Last modified February 9, 2010. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: BSU15450
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

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. 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

Subcellular location

Cell membrane; Multi-pass membrane protein HAMAP MF_00161.

Sequence similarities

Belongs to the peptidase A8 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
   Molecular functionAspartyl protease
Hydrolase
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: HAMAP

   Molecular functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 154154Lipoprotein signal peptidase HAMAP MF_00161
PRO_0000178769

Regions

Topological domain11Cytoplasmic Potential
Transmembrane2 – 2221 Potential
Topological domain23 – 5129Extracellular Potential
Transmembrane52 – 7221 Potential
Topological domain73 – 8412Cytoplasmic Potential
Transmembrane85 – 10521 Potential
Topological domain106 – 12318Extracellular Potential
Transmembrane124 – 14421 Potential
Topological domain145 – 15410Cytoplasmic Potential

Sites

Active site1021 Probable
Active site1291 Probable

Sequences

Sequence LengthMass (Da)Tools
Q45479-1 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 9229CD9FCA8CBB55

FASTA15417,427
        10         20         30         40         50         60 
MLYYMIALLI IAADQLTKWL VVKNMELGQS IPIIDQVFYI TSHRNTGAAW GILAGQMWFF 

        70         80         90        100        110        120 
YLITTAVIIG IVYYIQRYTK GQRLLGVALG LMLGGAIGNF IDRAVRQEVV DFIHVIIVNY 

       130        140        150 
NYPIFNIADS SLCVGVMLLF IQMLLDSGKK KKEQ 

« Hide

References

« Hide 'large scale' references
[1]"The signal peptidase II (lsp) gene of Bacillus subtilis."
Pragai Z., Tjalsma H., Bolhuis A., van Dijl J.M., Venema G., Bron S.
Microbiology 143:1327-1333(1997) [PubMed: 9141696] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]Baek-Rak L., Jeong-Hyun K.
Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
[4]"The potential active site of the lipoprotein-specific (type II) signal peptidase of Bacillus subtilis."
Tjalsma H., Zanen G., Venema G., Bron S., van Dijl J.M.
J. Biol. Chem. 274:28191-28197(1999) [PubMed: 10497172] [Abstract]
Cited for: MUTAGENESIS, ACTIVE SITES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U48870 Genomic DNA. Translation: AAB57766.1.
AL009126 Genomic DNA. Translation: CAB13419.1.
U08116 Unassigned DNA. No translation available.
PIRG69653.
RefSeqNP_389428.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSA08.001.

Genome annotation databases

GeneID938172.
GenomeReviewsGene locus BSU15450 in contig AL009126_GR.
KEGGbsu:BSU15450.
NMPDRfig|224308.1.peg.1547.

Organism-specific databases

SubtiListBG11793. lspA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMHBG724422.
OMADQASKRW.
PhylomeDBQ45479.

Enzyme and pathway databases

BRENDA3.4.23.36. 150.

Family and domain databases

HAMAPMF_00161. LspA.
[Tree]
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_BACSU
AccessionPrimary (citable) accession number: Q45479
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 9, 2010
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents