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P0AG96

- SECE_ECOLI

UniProt

P0AG96 - SECE_ECOLI

Protein

Protein translocase subunit SecE

Gene

secE

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

    Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of SecY.1 Publication

    GO - Molecular functioni

    1. P-P-bond-hydrolysis-driven protein transmembrane transporter activity Source: InterPro

    GO - Biological processi

    1. intracellular protein transmembrane transport Source: EcoliWiki
    2. intracellular protein transport Source: EcoliWiki
    3. protein secretion Source: UniProtKB-HAMAP
    4. protein targeting Source: UniProtKB-HAMAP
    5. protein transport by the Sec complex Source: EcoliWiki

    Keywords - Biological processi

    Protein transport, Translocation, Transport

    Enzyme and pathway databases

    BioCyciEcoCyc:SECE.
    ECOL316407:JW3944-MONOMER.

    Protein family/group databases

    TCDBi3.A.5.1.1. the general secretory pathway (sec) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein translocase subunit SecEUniRule annotation
    Gene namesi
    Name:secEUniRule annotation
    Synonyms:prlG
    Ordered Locus Names:b3981, JW3944
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10939. secE.

    Subcellular locationi

    Cell inner membrane 1 PublicationUniRule annotation; Multi-pass membrane protein 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cell envelope Sec protein transport complex Source: EcoCyc
    2. integral component of membrane Source: EcoliWiki
    3. integral component of plasma membrane Source: EcoCyc
    4. intracellular Source: GOC
    5. plasma membrane Source: EcoliWiki

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Essential; deletion experiments lead to loss of the SecYEG tranlocation channel. Leads to loss of translocation of lipoproteins Lpp and BRP (PubMed:15140892) and accumulation of signal peptidase I (lepB) in a soluble fraction (PubMed:21778229).2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi120 – 1201S → C: Massive ion flux when cross-linked to SecY C-67 mutation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 127127Protein translocase subunit SecEPRO_0000104163Add
    BLAST

    Post-translational modificationi

    Degraded by FtsH when the SecYEG complex is jammed or upon treatment with antibiotics that block translation elongation such as chloramphenicol.

    Proteomic databases

    PaxDbiP0AG96.
    PRIDEiP0AG96.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AG96.

    Interactioni

    Subunit structurei

    Part of the essential Sec protein translocation complex which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC/OxaA. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. The channel interacts with SecA via subunit SecY. SecE might contact ribosomal protein L23 and/or L29 when the translocation complex is docked with the ribosome.2 Publications

    Protein-protein interaction databases

    DIPiDIP-59303N.
    IntActiP0AG96. 2 interactions.
    STRINGi511145.b3981.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AKHelectron microscopy14.90C/Z17-127[»]
    2AKIelectron microscopy14.90C/Z17-127[»]
    3J01electron microscopy-B12-127[»]
    3J45electron microscopy9.50E74-127[»]
    3J46electron microscopy10.10E74-127[»]
    ProteinModelPortaliP0AG96.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AG96.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1919Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini33 – 4816Periplasmic1 PublicationAdd
    BLAST
    Topological domaini61 – 9737Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini116 – 12712Periplasmic1 PublicationAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei20 – 3213HelicalCuratedAdd
    BLAST
    Transmembranei49 – 6012HelicalCuratedAdd
    BLAST
    Transmembranei98 – 11518HelicalCuratedAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SecE/SEC61-gamma family.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0690.
    HOGENOMiHOG000219148.
    KOiK03073.
    OMAiTRPEATQ.
    OrthoDBiEOG6DRPR4.

    Family and domain databases

    HAMAPiMF_00422. SecE.
    InterProiIPR022943. SecE.
    IPR005807. SecE_bac.
    IPR001901. Translocase_SecE/Sec61-g.
    [Graphical view]
    PfamiPF00584. SecE. 1 hit.
    [Graphical view]
    PRINTSiPR01650. SECETRNLCASE.
    TIGRFAMsiTIGR00964. secE_bact. 1 hit.
    PROSITEiPS01067. SECE_SEC61G. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0AG96-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSANTEAQGS GRGLEAMKWV VVVALLLVAI VGNYLYRDIM LPLRALAVVI    50
    LIAAAGGVAL LTTKGKATVA FAREARTEVR KVIWPTRQET LHTTLIVAAV 100
    TAVMSLILWG LDGILVRLVS FITGLRF 127
    Length:127
    Mass (Da):13,643
    Last modified:December 20, 2005 - v1
    Checksum:i94D37280522875CE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30610 Genomic DNA. Translation: AAA24621.1.
    U00006 Genomic DNA. Translation: AAC43079.1.
    U00096 Genomic DNA. Translation: AAC76955.1.
    AP009048 Genomic DNA. Translation: BAE77339.1.
    PIRiA35139. VXECSE.
    RefSeqiNP_418408.1. NC_000913.3.
    YP_491480.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76955; AAC76955; b3981.
    BAE77339; BAE77339; BAE77339.
    GeneIDi12930517.
    948486.
    KEGGiecj:Y75_p3216.
    eco:b3981.
    PATRICi32123483. VBIEscCol129921_4094.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30610 Genomic DNA. Translation: AAA24621.1 .
    U00006 Genomic DNA. Translation: AAC43079.1 .
    U00096 Genomic DNA. Translation: AAC76955.1 .
    AP009048 Genomic DNA. Translation: BAE77339.1 .
    PIRi A35139. VXECSE.
    RefSeqi NP_418408.1. NC_000913.3.
    YP_491480.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AKH electron microscopy 14.90 C/Z 17-127 [» ]
    2AKI electron microscopy 14.90 C/Z 17-127 [» ]
    3J01 electron microscopy - B 12-127 [» ]
    3J45 electron microscopy 9.50 E 74-127 [» ]
    3J46 electron microscopy 10.10 E 74-127 [» ]
    ProteinModelPortali P0AG96.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59303N.
    IntActi P0AG96. 2 interactions.
    STRINGi 511145.b3981.

    Protein family/group databases

    TCDBi 3.A.5.1.1. the general secretory pathway (sec) family.

    Proteomic databases

    PaxDbi P0AG96.
    PRIDEi P0AG96.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76955 ; AAC76955 ; b3981 .
    BAE77339 ; BAE77339 ; BAE77339 .
    GeneIDi 12930517.
    948486.
    KEGGi ecj:Y75_p3216.
    eco:b3981.
    PATRICi 32123483. VBIEscCol129921_4094.

    Organism-specific databases

    EchoBASEi EB0932.
    EcoGenei EG10939. secE.

    Phylogenomic databases

    eggNOGi COG0690.
    HOGENOMi HOG000219148.
    KOi K03073.
    OMAi TRPEATQ.
    OrthoDBi EOG6DRPR4.

    Enzyme and pathway databases

    BioCyci EcoCyc:SECE.
    ECOL316407:JW3944-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AG96.
    PROi P0AG96.

    Gene expression databases

    Genevestigatori P0AG96.

    Family and domain databases

    HAMAPi MF_00422. SecE.
    InterProi IPR022943. SecE.
    IPR005807. SecE_bac.
    IPR001901. Translocase_SecE/Sec61-g.
    [Graphical view ]
    Pfami PF00584. SecE. 1 hit.
    [Graphical view ]
    PRINTSi PR01650. SECETRNLCASE.
    TIGRFAMsi TIGR00964. secE_bact. 1 hit.
    PROSITEi PS01067. SECE_SEC61G. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The secE gene encodes an integral membrane protein required for protein export in Escherichia coli."
      Schatz P.J., Riggs P.D., Jacq A., Fath M.J., Beckwith J.
      Genes Dev. 3:1035-1044(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon."
      Downing W.L., Sullivan S.L., Gottesman M.E., Dennis P.P.
      J. Bacteriol. 172:1621-1627(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery."
      Schatz P.J., Bieker K.L., Ottemann K.M., Silhavy T.J., Beckwith J.
      EMBO J. 10:1749-1757(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    7. "Evaluating the oligomeric state of SecYEG in preprotein translocase."
      Yahr T.L., Wickner W.T.
      EMBO J. 19:4393-4401(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    8. "SecYEG assembles into a tetramer to form the active protein translocation channel."
      Manting E.H., van Der Does C., Remigy H., Engel A., Driessen A.J.
      EMBO J. 19:852-861(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    9. "Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway."
      Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.
      J. Biol. Chem. 279:31026-31032(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN LIPOPROTEIN EXPORT, DISRUPTION PHENOTYPE.
    10. "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: SUBCELLULAR LOCATION.
      Strain: K12 / MG1655 / ATCC 47076.
    11. "The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE."
      Flower A.M., Osborne R.S., Silhavy T.J.
      EMBO J. 14:884-893(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTANTS.
    12. "Determining the conductance of the SecY protein translocation channel for small molecules."
      Saparov S.M., Erlandson K., Cannon K., Schaletzky J., Schulman S., Rapoport T.A., Pohl P.
      Mol. Cell 26:501-509(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF CHANNEL OPENING, MUTAGENESIS OF SER-120.
    13. "Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY."
      van Stelten J., Silva F., Belin D., Silhavy T.J.
      Science 325:753-756(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPLEX DEGRADATION.
      Strain: K12 / MC4100.
    14. "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: DISRUPTION PHENOTYPE.
      Strain: K12 / MG1655 / ATCC 47076.
    15. "Structure of the E. coli protein-conducting channel bound to a translating ribosome."
      Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III, Ban N., Frank J.
      Nature 438:318-324(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (14.9 ANGSTROMS) OF 17-127 IN COMPLEX WITH THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAIN.
      Strain: MRE-600.
    16. Cited for: STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAIN.
    17. "Protein translocation across the bacterial cytoplasmic membrane."
      Driessen A.J., Nouwen N.
      Annu. Rev. Biochem. 77:643-667(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiSECE_ECOLI
    AccessioniPrimary (citable) accession number: P0AG96
    Secondary accession number(s): P16920, Q2M8R7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3