true2005-12-202024-03-27136SECE_ECOLIThe 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.doi:10.1101/gad.3.7.10351989Genes Dev.31035-1044NUCLEOTIDE SEQUENCE [GENOMIC DNA]Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon.Downing W.L.Sullivan S.L.Gottesman M.E.Dennis P.P.doi:10.1128/jb.172.3.1621-1627.19901990J. Bacteriol.1721621-1627NUCLEOTIDE SEQUENCE [GENOMIC DNA]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. IIISofia H.J.Daniels D.L.doi:10.1093/nar/21.23.54081993Nucleic Acids Res.215408-5417NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]K12 / MG1655 / ATCC 47076The complete genome sequence of Escherichia coli K-12.Blattner F.R.Plunkett G. IIIBloch 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.doi:10.1126/science.277.5331.14531997Science2771453-1462NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]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.doi:10.1038/msb41000492006Mol. Syst. Biol.2E1-E5NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]K12 / W3110 / ATCC 27325 / DSM 5911One 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.doi:10.1002/j.1460-2075.1991.tb07699.x1991EMBO J.101749-1757TOPOLOGYEvaluating the oligomeric state of SecYEG in preprotein translocase.Yahr T.L.Wickner W.T.doi:10.1093/emboj/19.16.43932000EMBO J.194393-4401SUBUNITSecYEG 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.doi:10.1093/emboj/19.5.8522000EMBO J.19852-861SUBUNITTargeting 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.doi:10.1074/jbc.m4032292002004J. Biol. Chem.27931026-31032FUNCTION IN LIPOPROTEIN EXPORTDISRUPTION PHENOTYPEGlobal topology analysis of the Escherichia coli inner membrane proteome.Daley D.O.Rapp M.Granseth E.Melen K.Drew D.von Heijne G.doi:10.1126/science.11097302005Science3081321-1323SUBCELLULAR LOCATIONThe 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.doi:10.1002/j.1460-2075.1995.tb07070.x1995EMBO J.14884-893MUTANTSDetermining 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.doi:10.1016/j.molcel.2007.03.0222007Mol. Cell26501-509CHARACTERIZATION OF CHANNEL OPENINGMUTAGENESIS OF SER-120Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY.van Stelten J.Silva F.Belin D.Silhavy T.J.doi:10.1126/science.11722212009Science325753-756COMPLEX DEGRADATIONK12 / MC4100Membrane localization of small proteins in Escherichia coli.Fontaine F.Fuchs R.T.Storz G.doi:10.1074/jbc.m111.2456962011J. Biol. Chem.28632464-32474DISRUPTION PHENOTYPEMembrane protein insertion and assembly by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC.Komar J.Alvira S.Schulze R.J.Martin R.Lycklama a Nijeholt J.A.Lee S.C.Dafforn T.R.Deckers-Hebestreit G.Berger I.Schaffitzel C.Collinson I.doi:10.1042/bcj201605452016Biochem. J.4733341-3354FUNCTIONSUBUNITSUBCELLULAR LOCATIONBL21-DE3Structure 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. IIIBan N.Frank J.doi:10.1038/nature041332005Nature438318-324STRUCTURE BY ELECTRON MICROSCOPY (14.9 ANGSTROMS) OF 17-127 IN COMPLEX WITH THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAINMRE-600Cryo-EM structure of the ribosome-SecYE complex in the membrane environment.Frauenfeld J.Gumbart J.Sluis E.O.Funes S.Gartmann M.Beatrix B.Mielke T.Berninghausen O.Becker T.Schulten K.Beckmann R.doi:10.1038/nsmb.20262011Nat. Struct. Mol. Biol.18614-621STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAINProtein translocation across the bacterial cytoplasmic membrane.Driessen A.J.Nouwen N.doi:10.1146/annurev.biochem.77.061606.1607472008Annu. Rev. Biochem.77643-667REVIEWVXECSE14.90C/Z=17-12714.90C/Z=17-1279.50E=74-12710.10E=74-127B=12-1273.33h=1-12714.00E=3-1274.80h=67-1226.00E=60-1272621Holo-translocon SecYEG-SecDF-YajC-YidC complexProtein-conducting channel SecYEG complex4the general secretory pathway (sec) familyBacteriaPreprotein translocase secy subunitSecESecE_bacSecE_sfTranslocase_SecE/Sec61-gsecE_bactPROTEIN TRANSLOCASE SUBUNIT SECEPROTEIN TRANSLOCASE SUBUNIT SECESecESECETRNLCASESECE_SEC61GProtein translocase subunit SecEsecEprlGb3981JW3944Essential 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.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 SecDF-YidC-YajC translocase forms a supercomplex with SecYEG, called the holo-translocon (HTL) (PubMed:27435098). The stoichiometry of the super complex may be SecYEG:YidC:SecDF 4:3:1, YajC is in the reconstituted complex (with SecDF) but as no antibody is available it could not be quantified (PubMed:27435098). 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.Degraded by FtsH when the SecYEG complex is jammed or upon treatment with antibiotics that block translation elongation such as chloramphenicol.Essential; deletion experiments lead to loss of the SecYEG translocation 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).Belongs to the SecE/SEC61-gamma family.Protein translocase subunit SecE136431127Cytoplasmic19Helical2032Periplasmic3348Helical4960Cytoplasmic6197Helical98115Periplasmic116Massive ion flux when cross-linked to SecYC-67 mutation.C1207987117false2false5secAsecY2005-12-20113643d7fac8c3b32b51f5695354313167117dMSANTEAQGSGRGLEAMKWVVVVALLLVAIVGNYLYRDIMLPLRALAVVILIAAAGGVALLTTKGKATVAFAREARTEVRKVIWPTRQETLHTTLIVAAVTAVMSLILWGLDGILVRLVSFITGLRFtruetruetruetruetruetruetruetruetruetruetruetruetrue