SECE_METJA
ID SECE_METJA Reviewed; 74 AA.
AC Q57817;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422};
DE AltName: Full=Protein transport protein Sec61 gamma subunit homolog {ECO:0000255|HAMAP-Rule:MF_00422};
GN Name=secE {ECO:0000255|HAMAP-Rule:MF_00422}; OrderedLocusNames=MJ0371;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 11-66 IN COMPLEX WITH SECY AND
RP SECG.
RX PubMed=14661030; DOI=10.1038/nature02218;
RA Van den Berg B., Clemons W.M. Jr., Collinson I., Modis Y., Hartmann E.,
RA Harrison S.C., Rapoport T.A.;
RT "X-ray structure of a protein-conducting channel.";
RL Nature 427:36-44(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=17531810; DOI=10.1016/j.molcel.2007.05.002;
RA Li W., Schulman S., Boyd D., Erlandson K., Beckwith J., Rapoport T.A.;
RT "The plug domain of the SecY protein stabilizes the closed state of the
RT translocation channel and maintains a membrane seal.";
RL Mol. Cell 26:511-521(2007).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.6 ANGSTROMS) OF 2-433 DOCKED ONTO THE
RP E.COLI RIBOSOME.
RX PubMed=18158904; DOI=10.1016/j.molcel.2007.10.034;
RA Menetret J.F., Schaletzky J., Clemons W.M. Jr., Osborne A.R.,
RA Skanland S.S., Denison C., Gygi S.P., Kirkpatrick D.S., Park E.,
RA Ludtke S.J., Rapoport T.A., Akey C.W.;
RT "Ribosome binding of a single copy of the SecY complex: implications for
RT protein translocation.";
RL Mol. Cell 28:1083-1092(2007).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (8.7 ANGSTROMS) OF 3-67 DOCKED ONTO DOG
RP RIBOSOMES.
RX PubMed=18611385; DOI=10.1016/j.str.2008.05.003;
RA Menetret J.F., Hegde R.S., Aguiar M., Gygi S.P., Park E., Rapoport T.A.,
RA Akey C.W.;
RT "Single copies of Sec61 and TRAP associate with a nontranslating mammalian
RT ribosome.";
RL Structure 16:1126-1137(2008).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY OF 28-67 DOCKED ONTO E.COLI RIBOSOMES.
RX PubMed=19913480; DOI=10.1016/j.str.2009.09.010;
RA Gumbart J., Trabuco L.G., Schreiner E., Villa E., Schulten K.;
RT "Regulation of the protein-conducting channel by a bound ribosome.";
RL Structure 17:1453-1464(2009).
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.
CC -!- SUBUNIT: Component of the Sec protein translocase complex. Heterotrimer
CC consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. The
CC heterotrimers can form oligomers, although 1 heterotrimer is thought to
CC be able to translocate proteins. Interacts with the ribosome. May
CC interact with SecDF, and other proteins may be involved.
CC {ECO:0000269|PubMed:14661030}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000255|HAMAP-
CC Rule:MF_00422}.
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DR EMBL; L77117; AAB98360.1; -; Genomic_DNA.
DR PIR; C64346; C64346.
DR RefSeq; WP_010869870.1; NC_000909.1.
DR PDB; 1RH5; X-ray; 3.20 A; B=1-74.
DR PDB; 1RHZ; X-ray; 3.50 A; B=1-74.
DR PDB; 2YXQ; X-ray; 3.50 A; B=1-74.
DR PDB; 2YXR; X-ray; 3.60 A; B=1-74.
DR PDB; 3BO0; EM; 9.60 A; B=28-67.
DR PDB; 3BO1; EM; 9.60 A; B=28-67.
DR PDB; 3DKN; EM; 8.70 A; B=3-67.
DR PDB; 4V4N; EM; 9.00 A; A7=1-67.
DR PDB; 4V7I; EM; -; B=28-67.
DR PDBsum; 1RH5; -.
DR PDBsum; 1RHZ; -.
DR PDBsum; 2YXQ; -.
DR PDBsum; 2YXR; -.
DR PDBsum; 3BO0; -.
DR PDBsum; 3BO1; -.
DR PDBsum; 3DKN; -.
DR PDBsum; 4V4N; -.
DR PDBsum; 4V7I; -.
DR AlphaFoldDB; Q57817; -.
DR SMR; Q57817; -.
DR IntAct; Q57817; 2.
DR MINT; Q57817; -.
DR STRING; 243232.MJ_0371; -.
DR TCDB; 3.A.5.7.4; the general secretory pathway (sec) family.
DR EnsemblBacteria; AAB98360; AAB98360; MJ_0371.
DR GeneID; 1451228; -.
DR KEGG; mja:MJ_0371; -.
DR eggNOG; arCOG02204; Archaea.
DR HOGENOM; CLU_191921_0_0_2; -.
DR InParanoid; Q57817; -.
DR OMA; DFLHQCR; -.
DR OrthoDB; 121918at2157; -.
DR EvolutionaryTrace; Q57817; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0009306; P:protein secretion; IEA:UniProtKB-UniRule.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.5.820; -; 1.
DR HAMAP; MF_00422; SecE; 1.
DR InterPro; IPR023391; Prot_translocase_SecE_dom_sf.
DR InterPro; IPR008158; Translocase_Sec61-g.
DR InterPro; IPR001901; Translocase_SecE/Sec61-g.
DR Pfam; PF00584; SecE; 1.
DR SUPFAM; SSF103456; SSF103456; 1.
DR TIGRFAMs; TIGR00327; secE_euk_arch; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..74
FT /note="Protein translocase subunit SecE"
FT /id="PRO_0000104219"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT TRANSMEM 37..62
FT /note="Helical"
FT TOPO_DOM 63..74
FT /note="Extracellular"
FT HELIX 14..24
FT /evidence="ECO:0007829|PDB:1RH5"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 31..66
FT /evidence="ECO:0007829|PDB:1RH5"
SQ SEQUENCE 74 AA; 8438 MW; 10474AE938CC0ECD CRC64;
MKTDFNQKIE QLKEFIEECR RVWLVLKKPT KDEYLAVAKV TALGISLLGI IGYIIHVPAT
YIKGILKPPT TPRV
