SECY_SULAC
ID SECY_SULAC Reviewed; 463 AA.
AC P49978; Q4JB63;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 115.
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=Saci_0574;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=7495856; DOI=10.1016/0167-4781(95)00165-d;
RA Kath T., Schaefer G.;
RT "A secY homologous gene in the crenarchaeon Sulfolobus acidocaldarius.";
RL Biochim. Biophys. Acta 1264:155-158(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=10381320; DOI=10.1006/mpev.1998.0607;
RA Yang D., Kusser I., Koepke A.K., Koop B.F., Matheson A.T.;
RT "The structure and evolution of the ribosomal proteins encoded in the spc
RT operon of the archaeon (Crenarchaeota) Sulfolobus acidocaldarius.";
RL Mol. Phylogenet. Evol. 12:177-185(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
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; X85020; CAA59382.1; -; Genomic_DNA.
DR EMBL; Y07778; CAA69100.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY79966.1; -; Genomic_DNA.
DR PIR; S59968; S59968.
DR RefSeq; WP_011277468.1; NC_007181.1.
DR AlphaFoldDB; P49978; -.
DR SMR; P49978; -.
DR STRING; 330779.Saci_0574; -.
DR EnsemblBacteria; AAY79966; AAY79966; Saci_0574.
DR GeneID; 3473212; -.
DR KEGG; sai:Saci_0574; -.
DR PATRIC; fig|330779.12.peg.553; -.
DR eggNOG; arCOG04169; Archaea.
DR HOGENOM; CLU_031763_2_1_2; -.
DR OMA; KWGIGSG; -.
DR Proteomes; UP000001018; 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 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..463
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131770"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 21..47
FT /note="Helical; Name=Helix 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 48..60
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 61..89
FT /note="Discontinuously helical; Name=Helix 2"
FT /evidence="ECO:0000250"
FT INTRAMEM 61..68
FT /note="Helical; Name=Helix 2A"
FT /evidence="ECO:0000250"
FT INTRAMEM 69..80
FT /evidence="ECO:0000250"
FT INTRAMEM 81..89
FT /note="Helical; Name=Helix 2B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 90..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 111..134
FT /note="Helical; Name=Helix 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 135..142
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 143..167
FT /note="Helical; Name=Helix 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 168..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 175..193
FT /note="Helical; Name=Helix 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 194..236
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 237..258
FT /note="Helical; Name=Helix 6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 259..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 284..305
FT /note="Helical; Name=Helix 7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 306..341
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 342..361
FT /note="Helical; Name=Helix 8"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 362..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 405..423
FT /note="Helical; Name=Helix 9"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 424..426
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 427..441
FT /note="Helical; Name=Helix 10"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 442..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 463 AA; 50242 MW; 8B8CA9065C3C8E43 CRC64;
MGFMDFLAKM GENLPAVSKP KDKPTLTRKL LWTFIGLIVY LLMASIPLYG VTSSNSFLSN
FLAQQIIFAS SQGTLAQLGI GPVITSGLIM QILVGSKLIN VDLTTQEGKS KFTQAEKALA
LIFIIVESSL FGYVFTRATS NILLPIIVVV QLIIASYIIL LLDEMIQKGW GLGSGVSLFI
MAGIMKVIFW NMFGIVSVQS QNLPVGFFPL LVSYITSGRN LQEIVLNTSS TTPYQPDLIG
LIATVGLTIL IVYLVNTNIY IPVTTQRLRG IRTTVPLNFL YVSSIPVIFV SVLGADIQLF
ASLANSISNS ASGILTDIAN AFFFPPQGVP HSVYALVVDP VGAAIYAAVF IVLSIVFGML
WIDVAGLDPK TQAEQMIRSG IEIPGMRTNP RIIEGILSKY IYALGFFSSL IVGLIAVVAT
FLGTYGTGVG LLLAITIAMQ YYNLLAYERT LEMYPLLKRI VGE
