SECY_PYRHO
ID SECY_PYRHO Reviewed; 468 AA.
AC O59442;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 117.
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=PH1754;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA30868.1; -; Genomic_DNA.
DR PIR; E71184; E71184.
DR RefSeq; WP_010885818.1; NC_000961.1.
DR AlphaFoldDB; O59442; -.
DR SMR; O59442; -.
DR STRING; 70601.3258185; -.
DR EnsemblBacteria; BAA30868; BAA30868; BAA30868.
DR GeneID; 1442599; -.
DR KEGG; pho:PH1754; -.
DR eggNOG; arCOG04169; Archaea.
DR OMA; KWGIGSG; -.
DR OrthoDB; 13531at2157; -.
DR Proteomes; UP000000752; 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; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..468
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131769"
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..58
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 59..87
FT /note="Discontinuously helical; Name=Helix 2"
FT /evidence="ECO:0000250"
FT INTRAMEM 59..66
FT /note="Helical; Name=Helix 2A"
FT /evidence="ECO:0000250"
FT INTRAMEM 67..78
FT /evidence="ECO:0000250"
FT INTRAMEM 79..87
FT /note="Helical; Name=Helix 2B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 88..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 109..133
FT /note="Helical; Name=Helix 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 134..144
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 145..169
FT /note="Helical; Name=Helix 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 170..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 176..194
FT /note="Helical; Name=Helix 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 195..239
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 240..261
FT /note="Helical; Name=Helix 6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 262..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 286..307
FT /note="Helical; Name=Helix 7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 308..346
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 347..366
FT /note="Helical; Name=Helix 8"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 367..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 410..428
FT /note="Helical; Name=Helix 9"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 429..431
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 432..446
FT /note="Helical; Name=Helix 10"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 447..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 468 AA; 52314 MW; 707E102D59392C6C CRC64;
MGARDVIYAM EKWFPEVERP KKHVPLKEKF VWTGLALVLY YVLAEIPVYG IPKKIQDYFQ
FLRVVLAGRN GSILTLGIGP IVTAGIILQL LVGSELIRLD LANPEDRRFY QALQRVFSVF
MCFFEAAIWV LGGAFGRVGV DVTYTIATLM IIQLALGGII LIVLDELVSK WGIGSGISLF
IAAGVSQRIL TRSLNPLTDP NIIDPLTGKP AIVGAIPYFI QHILDGDLKG ALYRGGSAPD
MIAVTATIIV FLVVVYFESM RVEIPLGYRG VTIRGRYPIK FLYVSNIPII LTFALYANIQ
LWARVLDRFG HPWLGRFDPV TGNPIGGFVL YVIPPRNIFT VIDNPVRAII YLILTIIFSL
LFGFLWVELT GLDARTIARQ LQRAGLQIPG FRRDPRTLER VLQKYIPYVT FWGSLTVALI
SVLADFLGAL GTGTGILLTV GILYRFYEEI AREQITEMFP ALRRLFKG
