SECE_ECOLI
ID SECE_ECOLI Reviewed; 127 AA.
AC P0AG96; P16920; Q2M8R7;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422};
GN Name=secE {ECO:0000255|HAMAP-Rule:MF_00422}; Synonyms=prlG;
GN OrderedLocusNames=b3981, JW3944;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2673920; DOI=10.1101/gad.3.7.1035;
RA Schatz P.J., Riggs P.D., Jacq A., Fath M.J., Beckwith J.;
RT "The secE gene encodes an integral membrane protein required for protein
RT export in Escherichia coli.";
RL Genes Dev. 3:1035-1044(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2137819; DOI=10.1128/jb.172.3.1621-1627.1990;
RA Downing W.L., Sullivan S.L., Gottesman M.E., Dennis P.P.;
RT "Sequence and transcriptional pattern of the essential Escherichia coli
RT secE-nusG operon.";
RL J. Bacteriol. 172:1621-1627(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP TOPOLOGY.
RX PubMed=2050112; DOI=10.1002/j.1460-2075.1991.tb07699.x;
RA Schatz P.J., Bieker K.L., Ottemann K.M., Silhavy T.J., Beckwith J.;
RT "One of three transmembrane stretches is sufficient for the functioning of
RT the SecE protein, a membrane component of the E. coli secretion
RT machinery.";
RL EMBO J. 10:1749-1757(1991).
RN [7]
RP SUBUNIT.
RX PubMed=10944122; DOI=10.1093/emboj/19.16.4393;
RA Yahr T.L., Wickner W.T.;
RT "Evaluating the oligomeric state of SecYEG in preprotein translocase.";
RL EMBO J. 19:4393-4401(2000).
RN [8]
RP SUBUNIT.
RX PubMed=10698927; DOI=10.1093/emboj/19.5.852;
RA Manting E.H., van Der Does C., Remigy H., Engel A., Driessen A.J.;
RT "SecYEG assembles into a tetramer to form the active protein translocation
RT channel.";
RL EMBO J. 19:852-861(2000).
RN [9]
RP FUNCTION IN LIPOPROTEIN EXPORT, AND DISRUPTION PHENOTYPE.
RX PubMed=15140892; DOI=10.1074/jbc.m403229200;
RA Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.;
RT "Targeting and translocation of two lipoproteins in Escherichia coli via
RT the SRP/Sec/YidC pathway.";
RL J. Biol. Chem. 279:31026-31032(2004).
RN [10]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [11]
RP MUTANTS.
RX PubMed=7889938; DOI=10.1002/j.1460-2075.1995.tb07070.x;
RA Flower A.M., Osborne R.S., Silhavy T.J.;
RT "The allele-specific synthetic lethality of prlA-prlG double mutants
RT predicts interactive domains of SecY and SecE.";
RL EMBO J. 14:884-893(1995).
RN [12]
RP CHARACTERIZATION OF CHANNEL OPENING, AND MUTAGENESIS OF SER-120.
RX PubMed=17531809; DOI=10.1016/j.molcel.2007.03.022;
RA Saparov S.M., Erlandson K., Cannon K., Schaletzky J., Schulman S.,
RA Rapoport T.A., Pohl P.;
RT "Determining the conductance of the SecY protein translocation channel for
RT small molecules.";
RL Mol. Cell 26:501-509(2007).
RN [13]
RP COMPLEX DEGRADATION.
RC STRAIN=K12 / MC4100;
RX PubMed=19661432; DOI=10.1126/science.1172221;
RA van Stelten J., Silva F., Belin D., Silhavy T.J.;
RT "Effects of antibiotics and a proto-oncogene homolog on destruction of
RT protein translocator SecY.";
RL Science 325:753-756(2009).
RN [14]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21778229; DOI=10.1074/jbc.m111.245696;
RA Fontaine F., Fuchs R.T., Storz G.;
RT "Membrane localization of small proteins in Escherichia coli.";
RL J. Biol. Chem. 286:32464-32474(2011).
RN [15]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=27435098; DOI=10.1042/bcj20160545;
RA Komar J., Alvira S., Schulze R.J., Martin R., Lycklama a Nijeholt J.A.,
RA Lee S.C., Dafforn T.R., Deckers-Hebestreit G., Berger I., Schaffitzel C.,
RA Collinson I.;
RT "Membrane protein insertion and assembly by the bacterial holo-translocon
RT SecYEG-SecDF-YajC-YidC.";
RL Biochem. J. 473:3341-3354(2016).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (14.9 ANGSTROMS) OF 17-127 IN COMPLEX WITH
RP THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAIN.
RC STRAIN=MRE-600;
RX PubMed=16292303; DOI=10.1038/nature04133;
RA Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III,
RA Ban N., Frank J.;
RT "Structure of the E. coli protein-conducting channel bound to a translating
RT ribosome.";
RL Nature 438:318-324(2005).
RN [17]
RP STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH THE RIBOSOME AND A
RP NASCENT POLYPEPTIDE CHAIN.
RX PubMed=21499241; DOI=10.1038/nsmb.2026;
RA Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M., Beatrix B.,
RA Mielke T., Berninghausen O., Becker T., Schulten K., Beckmann R.;
RT "Cryo-EM structure of the ribosome-SecYE complex in the membrane
RT environment.";
RL Nat. Struct. Mol. Biol. 18:614-621(2011).
RN [18]
RP REVIEW.
RX PubMed=18078384; DOI=10.1146/annurev.biochem.77.061606.160747;
RA Driessen A.J., Nouwen N.;
RT "Protein translocation across the bacterial cytoplasmic membrane.";
RL Annu. Rev. Biochem. 77:643-667(2008).
CC -!- FUNCTION: Essential subunit of the protein translocation channel
CC SecYEG. Clamps together the 2 halves of SecY. May contact the channel
CC plug during translocation. Overexpression of some hybrid proteins has
CC been thought to jam the protein secretion apparatus resulting in cell
CC death; while this may be true it also results in FtsH-mediated
CC degradation of SecY. {ECO:0000269|PubMed:15140892}.
CC -!- SUBUNIT: Part of the essential Sec protein translocation complex which
CC comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC/OxaA.
CC Heterotrimer consisting of SecY, SecE and SecG subunits. The SecDF-
CC YidC-YajC translocase forms a supercomplex with SecYEG, called the
CC holo-translocon (HTL) (PubMed:27435098). The stoichiometry of the super
CC complex may be SecYEG:YidC:SecDF 4:3:1, YajC is in the reconstituted
CC complex (with SecDF) but as no antibody is available it could not be
CC quantified (PubMed:27435098). The heterotrimers can form oligomers,
CC although 1 heterotrimer is thought to be able to translocate proteins.
CC The channel interacts with SecA via subunit SecY. SecE might contact
CC ribosomal protein L23 and/or L29 when the translocation complex is
CC docked with the ribosome. {ECO:0000269|PubMed:10698927,
CC ECO:0000269|PubMed:10944122, ECO:0000269|PubMed:27435098}.
CC -!- INTERACTION:
CC P0AG96; P10408: secA; NbExp=2; IntAct=EBI-6404267, EBI-543213;
CC P0AG96; P0AGA2: secY; NbExp=5; IntAct=EBI-6404267, EBI-761422;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00422, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00422, ECO:0000269|PubMed:15919996}.
CC -!- PTM: Degraded by FtsH when the SecYEG complex is jammed or upon
CC treatment with antibiotics that block translation elongation such as
CC chloramphenicol.
CC -!- DISRUPTION PHENOTYPE: Essential; deletion experiments lead to loss of
CC the SecYEG translocation channel. Leads to loss of translocation of
CC lipoproteins Lpp and BRP (PubMed:15140892) and accumulation of signal
CC peptidase I (lepB) in a soluble fraction (PubMed:21778229).
CC {ECO:0000269|PubMed:15140892, ECO:0000269|PubMed:21778229}.
CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000255|HAMAP-
CC Rule:MF_00422}.
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DR EMBL; M30610; AAA24621.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43079.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76955.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77339.1; -; Genomic_DNA.
DR PIR; A35139; VXECSE.
DR RefSeq; NP_418408.1; NC_000913.3.
DR RefSeq; WP_001275702.1; NZ_STEB01000045.1.
DR PDB; 2AKH; EM; 14.90 A; C/Z=17-127.
DR PDB; 2AKI; EM; 14.90 A; C/Z=17-127.
DR PDB; 3J45; EM; 9.50 A; E=74-127.
DR PDB; 3J46; EM; 10.10 A; E=74-127.
DR PDB; 4V6M; EM; -; B=12-127.
DR PDB; 5GAE; EM; 3.33 A; h=1-127.
DR PDB; 5MG3; EM; 14.00 A; E=3-127.
DR PDB; 5NCO; EM; 4.80 A; h=67-122.
DR PDB; 6R7L; EM; 6.00 A; E=60-127.
DR PDBsum; 2AKH; -.
DR PDBsum; 2AKI; -.
DR PDBsum; 3J45; -.
DR PDBsum; 3J46; -.
DR PDBsum; 4V6M; -.
DR PDBsum; 5GAE; -.
DR PDBsum; 5MG3; -.
DR PDBsum; 5NCO; -.
DR PDBsum; 6R7L; -.
DR AlphaFoldDB; P0AG96; -.
DR SMR; P0AG96; -.
DR BioGRID; 4259511; 262.
DR BioGRID; 852780; 1.
DR ComplexPortal; CPX-1095; Holo-translocon SecYEG-SecDF-YajC-YidC complex.
DR ComplexPortal; CPX-1096; Protein-conducting channel SecYEG complex.
DR DIP; DIP-59303N; -.
DR IntAct; P0AG96; 4.
DR STRING; 511145.b3981; -.
DR TCDB; 3.A.5.1.1; the general secretory pathway (sec) family.
DR jPOST; P0AG96; -.
DR PaxDb; P0AG96; -.
DR PRIDE; P0AG96; -.
DR EnsemblBacteria; AAC76955; AAC76955; b3981.
DR EnsemblBacteria; BAE77339; BAE77339; BAE77339.
DR GeneID; 67415318; -.
DR GeneID; 948486; -.
DR KEGG; ecj:JW3944; -.
DR KEGG; eco:b3981; -.
DR PATRIC; fig|1411691.4.peg.2731; -.
DR EchoBASE; EB0932; -.
DR eggNOG; COG0690; Bacteria.
DR HOGENOM; CLU_113663_0_1_6; -.
DR InParanoid; P0AG96; -.
DR OMA; FLWLTDK; -.
DR PhylomeDB; P0AG96; -.
DR BioCyc; EcoCyc:SECE; -.
DR BioCyc; MetaCyc:SECE; -.
DR EvolutionaryTrace; P0AG96; -.
DR PRO; PR:P0AG96; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IDA:EcoCyc.
DR GO; GO:0006886; P:intracellular protein transport; IMP:EcoliWiki.
DR GO; GO:0032978; P:protein insertion into membrane from inner side; IDA:EcoCyc.
DR GO; GO:0009306; P:protein secretion; IEA:UniProtKB-UniRule.
DR GO; GO:0043952; P:protein transport by the Sec complex; IDA:ComplexPortal.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IDA:EcoCyc.
DR Gene3D; 1.20.5.1030; -; 1.
DR HAMAP; MF_00422; SecE; 1.
DR InterPro; IPR005807; SecE_bac.
DR InterPro; IPR038379; SecE_sf.
DR InterPro; IPR001901; Translocase_SecE/Sec61-g.
DR PANTHER; PTHR33910; PTHR33910; 1.
DR Pfam; PF00584; SecE; 1.
DR PRINTS; PR01650; SECETRNLCASE.
DR TIGRFAMs; TIGR00964; secE_bact; 1.
DR PROSITE; PS01067; SECE_SEC61G; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..127
FT /note="Protein translocase subunit SecE"
FT /id="PRO_0000104163"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:2050112"
FT TRANSMEM 20..32
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 33..48
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:2050112"
FT TRANSMEM 49..60
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 61..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:2050112"
FT TRANSMEM 98..115
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 116..127
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:2050112"
FT MUTAGEN 120
FT /note="S->C: Massive ion flux when cross-linked to SecY C-
FT 67 mutation."
FT /evidence="ECO:0000269|PubMed:17531809"
FT HELIX 61..79
FT /evidence="ECO:0007829|PDB:5GAE"
FT HELIX 87..117
FT /evidence="ECO:0007829|PDB:5GAE"
SQ SEQUENCE 127 AA; 13643 MW; 94D37280522875CE CRC64;
MSANTEAQGS GRGLEAMKWV VVVALLLVAI VGNYLYRDIM LPLRALAVVI LIAAAGGVAL
LTTKGKATVA FAREARTEVR KVIWPTRQET LHTTLIVAAV TAVMSLILWG LDGILVRLVS
FITGLRF
