SECY_METVA
ID SECY_METVA Reviewed; 438 AA.
AC P28541;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
DE AltName: Full=Protein transport protein SEC61 subunit alpha homolog {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465};
OS Methanococcus vannielii.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=2187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1764515; DOI=10.1016/0300-9084(91)90048-6;
RA Auer J., Spicker G., Boeck A.;
RT "Presence of a gene in the archaebacterium Methanococcus vannielii
RT homologous to secY of eubacteria.";
RL Biochimie 73:683-688(1991).
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 {ECO:0000255|HAMAP-Rule:MF_01465}.
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:0000255|HAMAP-Rule:MF_01465}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01465};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01465}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000255|HAMAP-
CC Rule:MF_01465}.
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DR EMBL; X62045; CAA43978.1; -; Genomic_DNA.
DR PIR; S24065; S24065.
DR AlphaFoldDB; P28541; -.
DR SMR; P28541; -.
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:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR10906; PTHR10906; 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 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..438
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131766"
FT TRANSMEM 1..43
FT /note="Helical; Name=Helix 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 44..54
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 55..83
FT /note="Discontinuously helical; Name=Helix 2"
FT /evidence="ECO:0000250"
FT INTRAMEM 55..62
FT /note="Helical; Name=Helix 2A"
FT /evidence="ECO:0000250"
FT INTRAMEM 63..74
FT /evidence="ECO:0000250"
FT INTRAMEM 75..83
FT /note="Helical; Name=Helix 2B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 84..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 105..129
FT /note="Helical; Name=Helix 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 130..136
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 137..161
FT /note="Helical; Name=Helix 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 162..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 168..186
FT /note="Helical; Name=Helix 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 187..209
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 210..231
FT /note="Helical; Name=Helix 6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 232..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 257..278
FT /note="Helical; Name=Helix 7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 279..315
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 316..335
FT /note="Helical; Name=Helix 8"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 336..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 379..397
FT /note="Helical; Name=Helix 9"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 398..400
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 401..415
FT /note="Helical; Name=Helix 10"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 416..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 438 AA; 47615 MW; A89B258DB44E946A CRC64;
MKIKPILELI PEVKRPLKGV SFKEKIQWTG LVLILYFILG TIDIYMGGAE MPAMFAFWQT
VTASKMGTLI TLGIGPIVTA GIIMQLLVGS ELISLDLSKP MNRALFQGLQ KLFGIFLCFL
EAVMFVGAGA FGVVNSTLAL ILVLQLALGA ILVIYLDEIV SRYGIGSGIG LFIAAGVAQT
IFVGAFGAEG YLWKFFSAMS VGSLGIAFEY ILPILSTLFV FLVVVYVESI RVEIPLAHGR
VKGAVGKYPI KFIYVSNLPV ILAAALFANI QLWGMFLDRM GYPILGQYSN GTAVSGIAYY
FSTPYGISNI ISDPLHAIFY TLMMVIFCIL FGLFWVETSG LDAKSMAKKL GNLDMAIKGF
RKSQKSIEQR LKRYIKPITV MGSAFVGFLA AAADFTGALG GGTGVLLTVS IVYRLYEQLV
QEQLSELHPA VAKFVGKR
