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Protein

Signal peptidase I

Gene

lepB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei91 – 911
Active sitei146 – 1461

GO - Molecular functioni

  • endopeptidase activity Source: EcoCyc
  • peptidase activity Source: EcoliWiki
  • serine-type endopeptidase activity Source: EcoCyc
  • toxic substance binding Source: EcoliWiki

GO - Biological processi

  • protein processing Source: EcoliWiki
  • proteolysis Source: EcoliWiki
  • signal peptide processing Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Enzyme and pathway databases

BioCyciEcoCyc:EG10530-MONOMER.
ECOL316407:JW2552-MONOMER.
MetaCyc:EG10530-MONOMER.
BRENDAi3.4.21.89. 2026.
SABIO-RKP00803.

Protein family/group databases

MEROPSiS26.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal peptidase I (EC:3.4.21.89)
Short name:
SPase I
Alternative name(s):
Leader peptidase I
Gene namesi
Name:lepB
Ordered Locus Names:b2568, JW2552
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10530. lepB.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 33PeriplasmicCurated
Transmembranei4 – 2219HelicalCuratedAdd
BLAST
Topological domaini23 – 5836CytoplasmicCuratedAdd
BLAST
Transmembranei59 – 7719HelicalCuratedAdd
BLAST
Topological domaini78 – 324247PeriplasmicCuratedAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: EcoliWiki
  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi62 – 621E → V: Indifferent.
Mutagenesisi78 – 781R → E, N or L: Indifferent.
Mutagenesisi91 – 911S → A: Loss of activity.
Mutagenesisi125 – 1251H → N: Indifferent.
Mutagenesisi128 – 1281R → Q: Small effect.
Mutagenesisi130 – 1301D → A: Indifferent.
Mutagenesisi144 – 1441Y → F: Indifferent.
Mutagenesisi146 – 1461K → M, D, G or S: Loss of activity.
Mutagenesisi147 – 1471R → Q: Small effect.
Mutagenesisi154 – 1541D → A: Loss of activity.
Mutagenesisi154 – 1541D → N: Indifferent.
Mutagenesisi159 – 1591D → N: Small effect.
Mutagenesisi171 – 1711C → A: Indifferent.
Mutagenesisi177 – 1771C → A: Indifferent.
Mutagenesisi236 – 2361H → N: Indifferent.
Mutagenesisi269 – 2691Y → F: Indifferent.
Mutagenesisi274 – 2741D → A: Indifferent.
Mutagenesisi276 – 2761R → Q: Small effect.
Mutagenesisi281 – 2811D → A: Indifferent.
Mutagenesisi283 – 2831R → Q: Small effect.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 324324Signal peptidase IPRO_0000109506Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Blocked amino end (Met)1 Publication
Disulfide bondi171 ↔ 177

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP00803.

Interactioni

Protein-protein interaction databases

STRINGi511145.b2568.

Structurei

Secondary structure

1
324
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi82 – 865Combined sources
Turni91 – 955Combined sources
Beta strandi100 – 11213Combined sources
Helixi114 – 1163Combined sources
Beta strandi119 – 1235Combined sources
Beta strandi131 – 1355Combined sources
Beta strandi142 – 1509Combined sources
Beta strandi155 – 1595Combined sources
Turni160 – 1634Combined sources
Beta strandi164 – 1685Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi189 – 19810Combined sources
Helixi200 – 2023Combined sources
Beta strandi205 – 2117Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi221 – 23111Combined sources
Beta strandi234 – 2407Combined sources
Helixi248 – 2503Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi268 – 2725Combined sources
Helixi282 – 2854Combined sources
Helixi290 – 2923Combined sources
Beta strandi293 – 30412Combined sources
Beta strandi310 – 3123Combined sources
Beta strandi313 – 3153Combined sources
Helixi317 – 3193Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00803.
SMRiP00803. Positions 78-324.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00803.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S26 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0681.
HOGENOMiHOG000003674.
InParanoidiP00803.
KOiK03100.
OMAiWVADKLV.
OrthoDBiEOG6KDKTM.
PhylomeDBiP00803.

Family and domain databases

Gene3Di2.10.109.10. 2 hits.
2.170.230.10. 1 hit.
InterProiIPR000223. 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]
PANTHERiPTHR12383. PTHR12383. 1 hit.
PfamiPF00717. Peptidase_S24. 1 hit.
PF10502. Peptidase_S26. 1 hit.
[Graphical view]
PRINTSiPR00727. LEADERPTASE.
SUPFAMiSSF51306. SSF51306. 1 hit.
TIGRFAMsiTIGR02227. sigpep_I_bact. 1 hit.
PROSITEiPS00501. SPASE_I_1. 1 hit.
PS00760. SPASE_I_2. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00803-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANMFALILV IATLVTGILW CVDKFFFAPK RRERQAAAQA AAGDSLDKAT
60 70 80 90 100
LKKVAPKPGW LETGASVFPV LAIVLIVRSF IYEPFQIPSG SMMPTLLIGD
110 120 130 140 150
FILVEKFAYG IKDPIYQKTL IETGHPKRGD IVVFKYPEDP KLDYIKRAVG
160 170 180 190 200
LPGDKVTYDP VSKELTIQPG CSSGQACENA LPVTYSNVEP SDFVQTFSRR
210 220 230 240 250
NGGEATSGFF EVPKNETKEN GIRLSERKET LGDVTHRILT VPIAQDQVGM
260 270 280 290 300
YYQQPGQQLA TWIVPPGQYF MMGDNRDNSA DSRYWGFVPE ANLVGRATAI
310 320
WMSFDKQEGE WPTGLRLSRI GGIH
Length:324
Mass (Da):35,960
Last modified:November 1, 1997 - v2
Checksum:i9419710D7212E660
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 432AG → R (PubMed:6311837).Curated
Sequence conflicti42 – 432AG → R (Ref. 2) Curated
Sequence conflicti123 – 1231T → N (PubMed:6311837).Curated
Sequence conflicti123 – 1231T → N (Ref. 2) Curated
Sequence conflicti183 – 1831V → A (PubMed:6311837).Curated
Sequence conflicti183 – 1831V → A (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00426 Genomic DNA. Translation: AAA24064.1.
D64044 Genomic DNA. Translation: BAA10915.1.
U00096 Genomic DNA. Translation: AAC75621.1.
AP009048 Genomic DNA. Translation: BAE76744.1.
PIRiG65034. ZPECS.
RefSeqiNP_417063.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC75621; AAC75621; b2568.
BAE76744; BAE76744; BAE76744.
GeneIDi947040.
KEGGiecj:Y75_p2521.
eco:b2568.
PATRICi32120535. VBIEscCol129921_2670.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K00426 Genomic DNA. Translation: AAA24064.1.
D64044 Genomic DNA. Translation: BAA10915.1.
U00096 Genomic DNA. Translation: AAC75621.1.
AP009048 Genomic DNA. Translation: BAE76744.1.
PIRiG65034. ZPECS.
RefSeqiNP_417063.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP00803.
SMRiP00803. Positions 78-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi511145.b2568.

Chemistry

BindingDBiP00803.
ChEMBLiCHEMBL4470.

Protein family/group databases

MEROPSiS26.001.

Proteomic databases

PRIDEiP00803.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75621; AAC75621; b2568.
BAE76744; BAE76744; BAE76744.
GeneIDi947040.
KEGGiecj:Y75_p2521.
eco:b2568.
PATRICi32120535. VBIEscCol129921_2670.

Organism-specific databases

EchoBASEiEB0525.
EcoGeneiEG10530. lepB.

Phylogenomic databases

eggNOGiCOG0681.
HOGENOMiHOG000003674.
InParanoidiP00803.
KOiK03100.
OMAiWVADKLV.
OrthoDBiEOG6KDKTM.
PhylomeDBiP00803.

Enzyme and pathway databases

BioCyciEcoCyc:EG10530-MONOMER.
ECOL316407:JW2552-MONOMER.
MetaCyc:EG10530-MONOMER.
BRENDAi3.4.21.89. 2026.
SABIO-RKP00803.

Miscellaneous databases

EvolutionaryTraceiP00803.
PROiP00803.

Family and domain databases

Gene3Di2.10.109.10. 2 hits.
2.170.230.10. 1 hit.
InterProiIPR000223. 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]
PANTHERiPTHR12383. PTHR12383. 1 hit.
PfamiPF00717. Peptidase_S24. 1 hit.
PF10502. Peptidase_S26. 1 hit.
[Graphical view]
PRINTSiPR00727. LEADERPTASE.
SUPFAMiSSF51306. SSF51306. 1 hit.
TIGRFAMsiTIGR02227. sigpep_I_bact. 1 hit.
PROSITEiPS00501. SPASE_I_1. 1 hit.
PS00760. SPASE_I_2. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiLEP_ECOLI
AccessioniPrimary (citable) accession number: P00803
Secondary accession number(s): P78098, Q2MAG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: June 24, 2015
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.