SECY_METJA
ID SECY_METJA Reviewed; 436 AA.
AC Q60175;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Protein translocase subunit SecY;
DE AltName: Full=Protein transport protein SEC61 subunit alpha homolog;
GN Name=secY; OrderedLocusNames=MJ0478;
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 1-423 IN COMPLEX WITH SECE 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) OF PLUG DELETION MUTANTS.
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
RP E.COLI RIBOSOMES.
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 2-433 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 2-433 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: The central subunit of the protein translocation channel
CC SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two
CC domains form a lateral gate at the front which open onto the bilayer
CC between TMs 2 and 7, and are clamped together by SecE at the back. The
CC channel is closed by both a pore ring composed of hydrophobic SecY
CC resides and a short helix (helix 2A) on the extracellular side of the
CC membrane which forms a plug. The plug probably moves laterally to allow
CC the channel to open. The ring and the pore may move independently.
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; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; L77117; AAB98469.1; -; Genomic_DNA.
DR RefSeq; WP_010869979.1; NC_000909.1.
DR PDB; 1RH5; X-ray; 3.20 A; A=1-436.
DR PDB; 1RHZ; X-ray; 3.50 A; A=1-436.
DR PDB; 2YXQ; X-ray; 3.50 A; A=1-436.
DR PDB; 2YXR; X-ray; 3.60 A; A=1-436.
DR PDB; 3BO0; EM; 9.60 A; A=2-433.
DR PDB; 3BO1; EM; 9.60 A; A=2-433.
DR PDB; 3DKN; EM; 8.70 A; A=2-433.
DR PDB; 4V4N; EM; 9.00 A; AX=1-436.
DR PDB; 4V7I; EM; -; A=2-433.
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; Q60175; -.
DR SMR; Q60175; -.
DR STRING; 243232.MJ_0478; -.
DR TCDB; 3.A.5.7.4; the general secretory pathway (sec) family.
DR EnsemblBacteria; AAB98469; AAB98469; MJ_0478.
DR GeneID; 1451340; -.
DR KEGG; mja:MJ_0478; -.
DR eggNOG; arCOG04169; Archaea.
DR HOGENOM; CLU_031763_3_0_2; -.
DR InParanoid; Q60175; -.
DR OMA; KWGIGSG; -.
DR OrthoDB; 13531at2157; -.
DR PhylomeDB; Q60175; -.
DR EvolutionaryTrace; Q60175; -.
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; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR Gene3D; 1.10.3370.10; -; 1.
DR HAMAP; MF_01465; SecY; 1.
DR InterPro; IPR026593; SecY.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR InterPro; IPR019561; Translocon_Sec61/SecY_plug_dom.
DR PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF10559; Plug_translocon; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 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..436
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131764"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT TRANSMEM 29..46
FT /note="Helical; Name=Helix 1"
FT TOPO_DOM 47..55
FT /note="Extracellular"
FT TRANSMEM 56..88
FT /note="Discontinuously helical; Name=Helix 2"
FT INTRAMEM 56..63
FT /note="Helical; Name=Helix 2A"
FT INTRAMEM 64..69
FT INTRAMEM 70..88
FT /note="Helical; Name=Helix 2B"
FT TOPO_DOM 89..110
FT /note="Cytoplasmic"
FT TRANSMEM 111..129
FT /note="Helical; Name=Helix 3"
FT TOPO_DOM 130..140
FT /note="Extracellular"
FT TRANSMEM 141..161
FT /note="Helical; Name=Helix 4"
FT TOPO_DOM 162..168
FT /note="Cytoplasmic"
FT TRANSMEM 169..191
FT /note="Helical; Name=Helix 5"
FT TOPO_DOM 192..209
FT /note="Extracellular"
FT TRANSMEM 210..227
FT /note="Helical; Name=Helix 6"
FT TOPO_DOM 228..255
FT /note="Cytoplasmic"
FT TRANSMEM 256..277
FT /note="Helical; Name=Helix 7"
FT TOPO_DOM 278..312
FT /note="Extracellular"
FT TRANSMEM 313..331
FT /note="Helical; Name=Helix 8"
FT TOPO_DOM 332..382
FT /note="Cytoplasmic"
FT TRANSMEM 383..397
FT /note="Helical; Name=Helix 9"
FT TOPO_DOM 398
FT /note="Extracellular"
FT TRANSMEM 399..412
FT /note="Helical; Name=Helix 10"
FT TOPO_DOM 413..436
FT /note="Cytoplasmic"
FT SITE 75
FT /note="Pore ring"
FT SITE 79
FT /note="Pore ring"
FT SITE 174
FT /note="Pore ring"
FT SITE 179
FT /note="Pore ring"
FT SITE 260
FT /note="Pore ring"
FT SITE 406
FT /note="Pore ring"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 23..40
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:2YXQ"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:1RH5"
FT TURN 70..75
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 76..91
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 101..128
FT /evidence="ECO:0007829|PDB:1RH5"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1RHZ"
FT HELIX 137..164
FT /evidence="ECO:0007829|PDB:1RH5"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 169..187
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:1RH5"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 211..226
FT /evidence="ECO:0007829|PDB:1RH5"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:1RH5"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1RH5"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:1RHZ"
FT HELIX 257..277
FT /evidence="ECO:0007829|PDB:1RH5"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:1RH5"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 313..338
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 342..348
FT /evidence="ECO:0007829|PDB:1RH5"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:1RHZ"
FT HELIX 363..395
FT /evidence="ECO:0007829|PDB:1RH5"
FT HELIX 402..419
FT /evidence="ECO:0007829|PDB:1RH5"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:1RHZ"
SQ SEQUENCE 436 AA; 47444 MW; 3E67747A7B5BDC0A CRC64;
MKKLIPILEK IPEVELPVKE ITFKEKLKWT GIVLVLYFIM GCIDVYTAGA QIPAIFEFWQ
TITASRIGTL ITLGIGPIVT AGIIMQLLVG SGIIQMDLSI PENRALFQGC QKLLSIIMCF
VEAVLFVGAG AFGILTPLLA FLVIIQIAFG SIILIYLDEI VSKYGIGSGI GLFIAAGVSQ
TIFVGALGPE GYLWKFLNSL IQGVPNIEYI APIIGTIIVF LMVVYAECMR VEIPLAHGRI
KGAVGKYPIK FVYVSNIPVI LAAALFANIQ LWGLALYRMG IPILGHYEGG RAVDGIAYYL
STPYGLSSVI SDPIHAIVYM IAMIITCVMF GIFWVETTGL DPKSMAKRIG SLGMAIKGFR
KSEKAIEHRL KRYIPPLTVM SSAFVGFLAT IANFIGALGG GTGVLLTVSI VYRMYEQLLR
EKVSELHPAI AKLLNK
