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P00803

- LEP_ECOLI

UniProt

P00803 - LEP_ECOLI

Protein

Signal peptidase I

Gene

lepB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    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

    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

    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 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00803.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei4 – 2219HelicalCuratedAdd
    BLAST
    Transmembranei59 – 7719HelicalCuratedAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S26 family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 432AG → R(PubMed:6311837)Curated
    Sequence conflicti42 – 432AG → R1 PublicationCurated
    Sequence conflicti123 – 1231T → N(PubMed:6311837)Curated
    Sequence conflicti123 – 1231T → N1 PublicationCurated
    Sequence conflicti183 – 1831V → A(PubMed:6311837)Curated
    Sequence conflicti183 – 1831V → A1 PublicationCurated

    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

    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: October 1, 2014
    This is version 144 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