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Reviewed, UniProtKB/Swiss-Prot P0A1W2 (LEP_SALTY)

Last modified February 9, 2010. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    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: STM2582
OrganismSalmonella typhimurium [Complete proteome] [HAMAP]
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

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

Subcellular location

Cell inner membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the peptidase S26 family.

Ontologies

Keywords
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
   Molecular functionHydrolase
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: UniProtKB-KW

   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 – 324324Signal peptidase I
PRO_0000109518

Regions

Topological domain1 – 33Periplasmic Potential
Transmembrane4 – 2219 Potential
Topological domain23 – 5836Cytoplasmic Potential
Transmembrane59 – 7719 Potential
Topological domain78 – 324247Periplasmic Potential

Sites

Active site911 By similarity
Active site1461 By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A1W2-1 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 40607CDA15779575

FASTA32435,778
        10         20         30         40         50         60 
MANMFALILV IATLVTGILW CVDKFVFAPK RRARQAAAQT ASGDALDNAT LNKVAPKPGW 

        70         80         90        100        110        120 
LETGASVFPV LAIVLIVRSF LYEPFQIPSG SMMPTLLIGD FILVEKFAYG IKDPIYQKTL 

       130        140        150        160        170        180 
IETGHPKRGD IVVFKYPEDP KLDYIKRAVG LPGDKITYDP VAKEVTIQPG CSSGQACENA 

       190        200        210        220        230        240 
LPVTYSNVEP SDFVQTFARR NGGEATSGFF EVPLNETKEN GIRLTERKET LGDVTHRILM 

       250        260        270        280        290        300 
VPIAQDQLGM YYQQPGQPLA TWVVPPGQYF MMGDNRDNSA DSRYWGFVPE ANLVGKAVAI 

       310        320 
WMSFDKQEGE WPTGVRLSRI GGIH 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the Salmonella typhimurium lep gene in Escherichia coli."
van Dijl J.M., van den Bergh R., Reversma T., Smith H., Bron S., Venema G.
Mol. Gen. Genet. 223:233-240(1990) [PubMed: 2250650] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: JM83.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X54933 Genomic DNA. Translation: CAA38694.1.
AE006468 Genomic DNA. Translation: AAL21476.1.
PIRS12020.
RefSeqNP_461517.1.

3D structure databases

SMRP0A1W2. Positions 78-324.
ModBaseSearch...

Proteomic databases

PRIDEP0A1W2.

Genome annotation databases

GeneID1254104.
GenomeReviewsGene locus STM2582 in contig AE006468_GR.
KEGGstm:STM2582.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG596607.
OMAVAVFKYP.

Enzyme and pathway databases

BioCycSTYP99287:STM2582-MONOMER.
BRENDA3.4.21.89. 2.

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.
IPR019756. Pept_S26A_signal_pept_1_Ser-AS.
IPR019759. Peptidase_S24_S26_cons-reg.
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. 1 hit.
PfamPF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSPR00727. LEADERPTASE.
TIGRFAMsTIGR02227. sigpep_I_bact. 1 hit.
PROSITEPS00501. SPASE_I_1. 1 hit.
PS00760. SPASE_I_2. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEP_SALTY
AccessionPrimary (citable) accession number: P0A1W2
Secondary accession number(s): P23697
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: February 9, 2010
This is version 44 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

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