SECY_ARCFU
ID SECY_ARCFU Reviewed; 493 AA.
AC O28377;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 124.
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}; OrderedLocusNames=AF_1902;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB89347.1; -; Genomic_DNA.
DR PIR; E69487; E69487.
DR RefSeq; WP_010879395.1; NC_000917.1.
DR AlphaFoldDB; O28377; -.
DR SMR; O28377; -.
DR STRING; 224325.AF_1902; -.
DR EnsemblBacteria; AAB89347; AAB89347; AF_1902.
DR GeneID; 24795646; -.
DR KEGG; afu:AF_1902; -.
DR eggNOG; arCOG04169; Archaea.
DR HOGENOM; CLU_031763_3_0_2; -.
DR OMA; KWGIGSG; -.
DR OrthoDB; 13531at2157; -.
DR PhylomeDB; O28377; -.
DR Proteomes; UP000002199; 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: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 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 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..493
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131760"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 22..48
FT /note="Helical; Name=Helix 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 49..59
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 60..88
FT /note="Discontinuously helical; Name=Helix 2"
FT /evidence="ECO:0000250"
FT INTRAMEM 60..67
FT /note="Helical; Name=Helix 2A"
FT /evidence="ECO:0000250"
FT INTRAMEM 68..79
FT /evidence="ECO:0000250"
FT INTRAMEM 80..88
FT /note="Helical; Name=Helix 2B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 89..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..134
FT /note="Helical; Name=Helix 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 135..151
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 152..176
FT /note="Helical; Name=Helix 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 177..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 183..201
FT /note="Helical; Name=Helix 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 202..244
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 245..266
FT /note="Helical; Name=Helix 6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 267..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 292..313
FT /note="Helical; Name=Helix 7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 314..367
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 368..387
FT /note="Helical; Name=Helix 8"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 388..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 431..449
FT /note="Helical; Name=Helix 9"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 450..454
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 455..469
FT /note="Helical; Name=Helix 10"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 470..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 493 AA; 53351 MW; 98B1C00AB8005FA5 CRC64;
MDSVIRALQP YFERIPSVER PKGHVHFREK FGWTAAILLL YFILSNVPVF GLSPESIDIF
AAYRALFAGS TGSIIALGIG PIVTASIILQ LLVGAGIIKL DLTNPEDRAA YQDFQRFLVF
VMIAVEAIPQ IAGGLLKPDL NLAAQLGVSP GIISFLIFIQ LFIGGVLIVY MDEVVSKWGI
GSGVSLFILA GIAQSIVVGL FNWVIPPNSA MPAGIIPRWI WIAQNYPLDQ LFTGSGLAFL
LIQGGILALI TTAAIILLVV FFEGTRVEIP LAHAVARGAR GRFPIKLIYA SVLPMIFVRA
LQANVVALGQ VLHARGVTIF GEFVNGKAVS GLMFFLQPVS SPYDWIPSLV KSQGAAFAAI
PDWMIYLHLL IDALILVVGG IIFAWFWVET SGMDARTVAS QIAKSGMQVP GFRKSPQVLE
RVLSRYIPKV TILGGAIIGI LTLVANMLGT IGNVSGTGLL LAVSIAYRFY EDLAKEQLTE
MHPLIRRMLG EEA
