SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00803

- LEP_ECOLI

UniProt

P00803 - LEP_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Signal peptidase I

Gene
lepB, b2568, JW2552
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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 – 9112 Publications
Active sitei146 – 14612 Publications

GO - Molecular functioni

  1. endopeptidase activity Source: EcoCyc
  2. peptidase activity Source: EcoliWiki
  3. serine-type endopeptidase activity Source: EcoCyc
  4. toxic substance binding Source: EcoliWiki

GO - Biological processi

  1. protein processing Source: EcoliWiki
  2. proteolysis Source: EcoliWiki
  3. 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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10530. lepB.

Subcellular locationi

Cell inner membrane; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 33Periplasmic Inferred
Transmembranei4 – 2219Helical; InferredAdd
BLAST
Topological domaini23 – 5836Cytoplasmic InferredAdd
BLAST
Transmembranei59 – 7719Helical; InferredAdd
BLAST
Topological domaini78 – 324247Periplasmic InferredAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: EcoliWiki
  2. integral component of plasma membrane Source: EcoCyc
  3. plasma membrane Source: EcoCyc
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.

Expressioni

Gene expression databases

GenevestigatoriP00803.

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 – 865
Turni91 – 955
Beta strandi100 – 11213
Helixi114 – 1163
Beta strandi119 – 1235
Beta strandi131 – 1355
Beta strandi142 – 1509
Beta strandi155 – 1595
Turni160 – 1634
Beta strandi164 – 1685
Beta strandi183 – 1853
Beta strandi189 – 19810
Helixi200 – 2023
Beta strandi205 – 2117
Beta strandi214 – 2163
Beta strandi221 – 23111
Beta strandi234 – 2407
Helixi248 – 2503
Beta strandi261 – 2633
Beta strandi268 – 2725
Helixi282 – 2854
Helixi290 – 2923
Beta strandi293 – 30412
Beta strandi308 – 3103
Beta strandi313 – 3153
Helixi317 – 3193

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP00803.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S26 family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0681.
HOGENOMiHOG000003674.
KOiK03100.
OMAiFKYPKDP.
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

MANMFALILV IATLVTGILW CVDKFFFAPK RRERQAAAQA AAGDSLDKAT    50
LKKVAPKPGW LETGASVFPV LAIVLIVRSF IYEPFQIPSG SMMPTLLIGD 100
FILVEKFAYG IKDPIYQKTL IETGHPKRGD IVVFKYPEDP KLDYIKRAVG 150
LPGDKVTYDP VSKELTIQPG CSSGQACENA LPVTYSNVEP SDFVQTFSRR 200
NGGEATSGFF EVPKNETKEN GIRLSERKET LGDVTHRILT VPIAQDQVGM 250
YYQQPGQQLA TWIVPPGQYF MMGDNRDNSA DSRYWGFVPE ANLVGRATAI 300
WMSFDKQEGE WPTGLRLSRI GGIH 324
Length:324
Mass (Da):35,960
Last modified:November 1, 1997 - v2
Checksum:i9419710D7212E660
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 432AG → R1 Publication
Sequence conflicti42 – 432AG → R1 Publication
Sequence conflicti123 – 1231T → N1 Publication
Sequence conflicti123 – 1231T → N1 Publication
Sequence conflicti183 – 1831V → A1 Publication
Sequence conflicti183 – 1831V → A1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_490796.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75621; AAC75621; b2568.
BAE76744; BAE76744; BAE76744.
GeneIDi12930473.
947040.
KEGGiecj:Y75_p2521.
eco:b2568.
PATRICi32120535. VBIEscCol129921_2670.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi G65034. ZPECS.
RefSeqi NP_417063.1. NC_000913.3.
YP_490796.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B12 X-ray 1.95 A/B/C/D 77-324 [» ]
1KN9 X-ray 2.40 A/B/C/D 77-324 [» ]
1T7D X-ray 2.47 A/B 76-324 [» ]
3IIQ X-ray 2.00 A/B 77-324 [» ]
3S04 X-ray 2.44 A/B 76-324 [» ]
ProteinModelPortali P00803.
SMRi P00803. Positions 78-324.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 511145.b2568.

Chemistry

ChEMBLi CHEMBL4470.

Protein family/group databases

MEROPSi S26.001.

Proteomic databases

PRIDEi P00803.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75621 ; AAC75621 ; b2568 .
BAE76744 ; BAE76744 ; BAE76744 .
GeneIDi 12930473.
947040.
KEGGi ecj:Y75_p2521.
eco:b2568.
PATRICi 32120535. VBIEscCol129921_2670.

Organism-specific databases

EchoBASEi EB0525.
EcoGenei EG10530. lepB.

Phylogenomic databases

eggNOGi COG0681.
HOGENOMi HOG000003674.
KOi K03100.
OMAi FKYPKDP.
OrthoDBi EOG6KDKTM.
PhylomeDBi P00803.

Enzyme and pathway databases

BioCyci EcoCyc:EG10530-MONOMER.
ECOL316407:JW2552-MONOMER.
MetaCyc:EG10530-MONOMER.
BRENDAi 3.4.21.89. 2026.
SABIO-RK P00803.

Miscellaneous databases

EvolutionaryTracei P00803.
PROi P00803.

Gene expression databases

Genevestigatori P00803.

Family and domain databases

Gene3Di 2.10.109.10. 2 hits.
2.170.230.10. 1 hit.
InterProi IPR000223. 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 ]
PANTHERi PTHR12383. PTHR12383. 1 hit.
Pfami PF00717. Peptidase_S24. 1 hit.
PF10502. Peptidase_S26. 1 hit.
[Graphical view ]
PRINTSi PR00727. LEADERPTASE.
SUPFAMi SSF51306. SSF51306. 1 hit.
TIGRFAMsi TIGR02227. sigpep_I_bact. 1 hit.
PROSITEi PS00501. SPASE_I_1. 1 hit.
PS00760. SPASE_I_2. 1 hit.
PS00761. SPASE_I_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 143 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