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P00803 (LEP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:b2568, JW2552
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 Ref.12.

Sequence similarities

Belongs to the peptidase S26 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 324324Signal peptidase I
PRO_0000109506

Regions

Topological domain1 – 33Periplasmic Probable
Transmembrane4 – 2219Helical; Probable
Topological domain23 – 5836Cytoplasmic Probable
Transmembrane59 – 7719Helical; Probable
Topological domain78 – 324247Periplasmic Probable

Sites

Active site911 Ref.7 Ref.9
Active site1461 Ref.7 Ref.9

Amino acid modifications

Modified residue11Blocked amino end (Met) Ref.1
Disulfide bond171 ↔ 177

Experimental info

Mutagenesis621E → V: Indifferent.
Mutagenesis781R → E, N or L: Indifferent.
Mutagenesis911S → A: Loss of activity.
Mutagenesis1251H → N: Indifferent.
Mutagenesis1281R → Q: Small effect.
Mutagenesis1301D → A: Indifferent.
Mutagenesis1441Y → F: Indifferent.
Mutagenesis1461K → M, D, G or S: Loss of activity.
Mutagenesis1471R → Q: Small effect.
Mutagenesis1541D → A: Loss of activity.
Mutagenesis1541D → N: Indifferent.
Mutagenesis1591D → N: Small effect.
Mutagenesis1711C → A: Indifferent.
Mutagenesis1771C → A: Indifferent.
Mutagenesis2361H → N: Indifferent.
Mutagenesis2691Y → F: Indifferent.
Mutagenesis2741D → A: Indifferent.
Mutagenesis2761R → Q: Small effect.
Mutagenesis2811D → A: Indifferent.
Mutagenesis2831R → Q: Small effect.
Sequence conflict42 – 432AG → R Ref.1
Sequence conflict42 – 432AG → R Ref.2
Sequence conflict1231T → N Ref.1
Sequence conflict1231T → N Ref.2
Sequence conflict1831V → A Ref.1
Sequence conflict1831V → A Ref.2

Secondary structure

.................................................. 324
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00803 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 9419710D7212E660

FASTA32435,960
        10         20         30         40         50         60 
MANMFALILV IATLVTGILW CVDKFFFAPK RRERQAAAQA AAGDSLDKAT LKKVAPKPGW 

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

       130        140        150        160        170        180 
IETGHPKRGD IVVFKYPEDP KLDYIKRAVG LPGDKVTYDP VSKELTIQPG CSSGQACENA 

       190        200        210        220        230        240 
LPVTYSNVEP SDFVQTFSRR NGGEATSGFF EVPKNETKEN GIRLSERKET LGDVTHRILT 

       250        260        270        280        290        300 
VPIAQDQVGM YYQQPGQQLA TWIVPPGQYF MMGDNRDNSA DSRYWGFVPE ANLVGRATAI 

       310        320 
WMSFDKQEGE WPTGLRLSRI GGIH 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope."
Wolfe P.B., Wickner W., Goodman J.M.
J. Biol. Chem. 258:12073-12080(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Nashimoto H., Saito N.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology."
von Heijne G.
EMBO J. 5:3021-3027(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY.
[6]"Mapping of catalytically important domains in Escherichia coli leader peptidase."
Bilgin N., Lee J.I., Zhu H.Y., Dalbey R., von Heijne G.
EMBO J. 9:2717-2722(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY.
[7]"Identification of potential active-site residues in the Escherichia coli leader peptidase."
Sung M., Dalbey R.E.
J. Biol. Chem. 267:13154-13159(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS, ACTIVE SITES.
[8]"On the catalytic mechanism of prokaryotic leader peptidase 1."
Black M.T., Munn J.G.R., Allsop A.E.
Biochem. J. 282:539-543(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
Strain: HJM114 and IT41.
[9]"Evidence that the catalytic activity of prokaryote leader peptidase depends upon the operation of a serine-lysine catalytic dyad."
Black M.T.
J. Bacteriol. 175:4957-4961(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS, ACTIVE SITES.
[10]"Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase."
San Millan J.L., Boyd D., Dalbey R., Wickner W., Beckwith J.
J. Bacteriol. 171:5536-5541(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY.
[11]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.
[12]"Membrane localization of small proteins in Escherichia coli."
Fontaine F., Fuchs R.T., Storz G.
J. Biol. Chem. 286:32464-32474(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: K12 / MG1655 / ATCC 47076.
[13]"Crystal structure of a bacterial signal peptidase in complex with a beta-lactam inhibitor."
Paetzel M., Dalbey R.E., Strynadka N.C.
Nature 396:186-190(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 77-324.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K00426 Genomic DNA. Translation: AAA24064.1.
D64044 Genomic DNA. Translation: BAA10915.1.
U00096 Genomic DNA. Translation: AAC75621.1.
AP009048 Genomic DNA. Translation: BAE76744.1.
PIRZPECS. G65034.
RefSeqNP_417063.1. NC_000913.3.
YP_490796.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B12X-ray1.95A/B/C/D77-324[»]
1KN9X-ray2.40A/B/C/D77-324[»]
1T7DX-ray2.47A/B76-324[»]
3IIQX-ray2.00A/B77-324[»]
3S04X-ray2.44A/B76-324[»]
ProteinModelPortalP00803.
SMRP00803. Positions 78-324.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511145.b2568.

Chemistry

ChEMBLCHEMBL4470.

Protein family/group databases

MEROPSS26.001.

Proteomic databases

PRIDEP00803.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75621; AAC75621; b2568.
BAE76744; BAE76744; BAE76744.
GeneID12930473.
947040.
KEGGecj:Y75_p2521.
eco:b2568.
PATRIC32120535. VBIEscCol129921_2670.

Organism-specific databases

EchoBASEEB0525.
EcoGeneEG10530. lepB.

Phylogenomic databases

eggNOGCOG0681.
HOGENOMHOG000003674.
KOK03100.
OMASPWFVYF.
OrthoDBEOG6KDKTM.
PhylomeDBP00803.
ProtClustDBPRK10861.

Enzyme and pathway databases

BioCycEcoCyc:EG10530-MONOMER.
ECOL316407:JW2552-MONOMER.
MetaCyc:EG10530-MONOMER.
BRENDA3.4.21.89. 2026.
SABIO-RKP00803.

Gene expression databases

GenevestigatorP00803.

Family and domain databases

Gene3D2.10.109.10. 2 hits.
2.170.230.10. 1 hit.
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.
IPR028360. Peptidase_S24/S26_b-rbn.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR019533. Peptidase_S26.
IPR019766. Peptidase_S26A_all-beta_subdom.
[Graphical view]
PANTHERPTHR12383. PTHR12383. 1 hit.
PfamPF00717. Peptidase_S24. 1 hit.
PF10502. Peptidase_S26. 1 hit.
[Graphical view]
PRINTSPR00727. LEADERPTASE.
SUPFAMSSF51306. SSF51306. 1 hit.
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...

Other

EvolutionaryTraceP00803.
PROP00803.

Entry information

Entry nameLEP_ECOLI
AccessionPrimary (citable) accession number: P00803
Secondary accession number(s): P78098, Q2MAG2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene