Skip Header

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

Q8L2J7 (LEP_RICTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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:
Signal peptidase I

Short name=SPase I
EC=3.4.21.89
Alternative name(s):
Leader peptidase I
Gene names
Name:lepB
Ordered Locus Names:RT0020
OrganismRickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]
Taxonomic identifier257363 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Complements E.coli mutants temperature-sensitive for lepB function.

Catalytic activity

Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.

Subcellular location

Cell inner membrane; Single-pass type II membrane protein Potential.

Sequence similarities

Belongs to the peptidase S26 family.

Ontologies

Keywords
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionserine-type peptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264Signal peptidase I
PRO_0000316278

Regions

Topological domain1 – 1818Cytoplasmic Potential
Transmembrane19 – 3921Helical; Potential
Topological domain40 – 264225Periplasmic Potential

Sites

Active site431 By similarity
Active site1061 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8L2J7 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: E35E28BD4585A002

FASTA26430,849
        10         20         30         40         50         60 
MNRDNTKTNK TVKQEFASFT FVICIALVIR ILIMEPFTVP TGSMKATILE NDYIFSTKYS 

        70         80         90        100        110        120 
YGYSNYSLSF FDFIPLFKGR VFAREPERGD IVVFRPPNDM SVRYIKRLIG LPGDKIQLID 

       130        140        150        160        170        180 
DVIYINDKKI ERTEVGTYIG EDGIKYLKFK ETLPNGRTYF SYKLAPIFGI ISNDRYSNTG 

       190        200        210        220        230        240 
VFYVPEGQYF FLGDNRDRSN DSRVNLGFVP FENFIGKAQF IWFSTKITWW DNDIGIINLI 

       250        260 
LKLKPWIESV RLSRIFKNLY NVDE 

« Hide

References

« Hide 'large scale' references
[1]"Molecular and functional analysis of the lepB gene, encoding a type I signal peptidase from Rickettsia rickettsii and Rickettsia typhi."
Rahman M.S., Simser J.A., Macaluso K.R., Azad A.F.
J. Bacteriol. 185:4578-4584(2003) [PubMed: 12867468] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION IN E.COLI.
Strain: Ethiopian AZ322.
[2]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed: 15317790] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF503336 Genomic DNA. Translation: AAM22228.1.
AE017197 Genomic DNA. Translation: AAU03508.1.
RefSeqYP_066990.1. NC_006142.1.

3D structure databases

HSSPHSSP built from PDB template 1B12 based on UniProtKB P00803.
ProteinModelPortalQ8L2J7.
ModBaseSearch...

Protein family/group databases

MEROPSS26.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2958484.
GenomeReviewsGene locus RT0020 in contig AE017197_GR.
KEGGrty:RT0020.
PATRIC17909190. VBIRicTyp34752_0018.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG596607.
OMAKPWIESV.
ProtClustDBCLSK870751.

Enzyme and pathway databases

BioCycRTYP257363:RT0020-MONOMER.

Family and domain databases

InterProIPR000223. Pept_S26A_signal_pept_1.
IPR019758. Pept_S26A_signal_pept_1_CS.
IPR019757. Pept_S26A_signal_pept_1_Lys-AS.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011056. Peptidase_S24_S26A/B/C_b-rbn.
[Graphical view]
Gene3DG3DSA:2.10.109.10. Pept_S24_S26_C. 2 hits.
KOK03100.
PfamPF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSPR00727. LEADERPTASE.
SUPFAMSSF51306. Pept_S24_S26_C. 1 hit.
TIGRFAMsTIGR02227. Sigpep_I_bact. 1 hit.
PROSITEPS00760. SPASE_I_2. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEP_RICTY
AccessionPrimary (citable) accession number: Q8L2J7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 69 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

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names

SIMILARITY comments

Index of protein domains and families