SECY_PYRFU
ID SECY_PYRFU Reviewed; 468 AA.
AC Q8U019;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Protein translocase subunit SecY;
DE AltName: Full=Protein transport protein SEC61 subunit alpha homolog;
GN Name=secY; OrderedLocusNames=PF1801;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE SECYE COMPLEX WITH AN OPEN
RP LATERAL GATE, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 454-GLN--ALA-468; 459-PHE--ALA-461 AND 463-ARG-LYS-464.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=20855604; DOI=10.1073/pnas.1012556107;
RA Egea P.F., Stroud R.M.;
RT "Lateral opening of a translocon upon entry of protein suggests the
RT mechanism of insertion into membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17182-17187(2010).
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 Complements an E.coli temperature-sensitive secY mutation; deletion of
CC the last 15 residues prevents complementation, which may indicate a
CC role of this region in translocation.
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. The beta
CC subunit (SecG) was lost during crystallization.
CC {ECO:0000269|PubMed:20855604}.
CC -!- INTERACTION:
CC Q8U019; Q8TZK2: secE; NbExp=5; IntAct=EBI-9025098, EBI-9025109;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20855604};
CC Multi-pass membrane protein {ECO:0000269|PubMed:20855604}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; AE009950; AAL81925.1; -; Genomic_DNA.
DR RefSeq; WP_011012942.1; NZ_CP023154.1.
DR PDB; 3MP7; X-ray; 2.90 A; A=1-468.
DR PDBsum; 3MP7; -.
DR AlphaFoldDB; Q8U019; -.
DR SMR; Q8U019; -.
DR DIP; DIP-59389N; -.
DR IntAct; Q8U019; 2.
DR STRING; 186497.PF1801; -.
DR TCDB; 3.A.5.7.2; the general secretory pathway (sec) family.
DR EnsemblBacteria; AAL81925; AAL81925; PF1801.
DR GeneID; 41713620; -.
DR KEGG; pfu:PF1801; -.
DR PATRIC; fig|186497.12.peg.1872; -.
DR eggNOG; arCOG04169; Archaea.
DR HOGENOM; CLU_031763_3_0_2; -.
DR OMA; KWGIGSG; -.
DR OrthoDB; 13531at2157; -.
DR PhylomeDB; Q8U019; -.
DR EvolutionaryTrace; Q8U019; -.
DR Proteomes; UP000001013; 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 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..468
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131768"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT TRANSMEM 34..48
FT /note="Helical; Name=Helix 1"
FT TOPO_DOM 49..57
FT /note="Extracellular"
FT TRANSMEM 58..88
FT /note="Discontinuously helical; Name=Helix 2"
FT INTRAMEM 58..71
FT /note="Helical; Name=Helix 2A"
FT INTRAMEM 72
FT INTRAMEM 73..88
FT /note="Helical; Name=Helix 2B"
FT TOPO_DOM 89..115
FT /note="Cytoplasmic"
FT TRANSMEM 116..130
FT /note="Helical; Name=Helix 3"
FT TOPO_DOM 131..148
FT /note="Extracellular"
FT TRANSMEM 149..166
FT /note="Helical; Name=Helix 4"
FT TOPO_DOM 167..176
FT /note="Cytoplasmic"
FT TRANSMEM 177..196
FT /note="Helical; Name=Helix 5"
FT TOPO_DOM 197..239
FT /note="Extracellular"
FT TRANSMEM 240..257
FT /note="Helical; Name=Helix 6"
FT TOPO_DOM 258..285
FT /note="Cytoplasmic"
FT TRANSMEM 286..303
FT /note="Helical; Name=Helix 7"
FT TOPO_DOM 304..346
FT /note="Extracellular"
FT TRANSMEM 347..363
FT /note="Helical; Name=Helix 8"
FT TOPO_DOM 364..407
FT /note="Cytoplasmic"
FT TRANSMEM 408..427
FT /note="Helical; Name=Helix 9"
FT TOPO_DOM 428
FT /note="Extracellular"
FT TRANSMEM 429..443
FT /note="Helical; Name=Helix 10"
FT TOPO_DOM 444..468
FT /note="Cytoplasmic"
FT SITE 78
FT /note="Pore ring"
FT SITE 82
FT /note="Pore ring"
FT SITE 177
FT /note="Pore ring"
FT SITE 181
FT /note="Pore ring"
FT SITE 291
FT /note="Pore ring"
FT SITE 438
FT /note="Pore ring"
FT MUTAGEN 454..468
FT /note="Missing: No longer complements secY24, an E.coli
FT temperature-sensitive secY mutation."
FT /evidence="ECO:0000269|PubMed:20855604"
FT MUTAGEN 459..461
FT /note="FPA->PPP: No longer complements secY24, an E.coli
FT temperature-sensitive secY mutation."
FT /evidence="ECO:0000269|PubMed:20855604"
FT MUTAGEN 463..464
FT /note="RK->AA: No longer complements secY24, an E.coli
FT temperature-sensitive secY mutation."
FT /evidence="ECO:0000269|PubMed:20855604"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:3MP7"
FT TURN 62..66
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:3MP7"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 147..171
FT /evidence="ECO:0007829|PDB:3MP7"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 176..193
FT /evidence="ECO:0007829|PDB:3MP7"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:3MP7"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 241..259
FT /evidence="ECO:0007829|PDB:3MP7"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 287..307
FT /evidence="ECO:0007829|PDB:3MP7"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:3MP7"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 345..369
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:3MP7"
FT TURN 390..395
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 409..427
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 434..457
FT /evidence="ECO:0007829|PDB:3MP7"
FT HELIX 459..464
FT /evidence="ECO:0007829|PDB:3MP7"
SQ SEQUENCE 468 AA; 52299 MW; 7969DCB9C1983F68 CRC64;
MGARDIIYAL ERWFPEVERP KRRVPLRERF MWTGVALILY YVLAEIPVYG IPERIQDYFQ
FLRVVLAGRN GSILTLGIGP IVTAGIILQL LVGSEIIKLD LANPEDRRFY QALQRVFSVF
MCFFEAAVWI LGGAFGRVGV DVTYAIAVLM ILQLAMGGIV LIILDELVSK WGIGSGISLF
IAAGVSQTIL TRSLNPLTDP NIIDPLTGQP AIVGAIPYFI QHILKGDLWG AIYRGGSAPD
MLSVVATIVV FFIVVYFESM RVEIPLGYRG VTVRGSYPIR FLYVSNIPII LTFALYANIQ
LWARVLDRLG HPWLGRFDPT TGSPISGFVL YVIPPRNIFS VIDNPVRAIV YLILTVIFSL
LFGYLWVELT GLDARSIARQ LQRAGLQIPG FRRDPRTLEK VLQRYIPYVT FWGSLTVALI
AVLADFLGAL GTGTGILLTV GILYRFYEEI AREQITEMFP ALRKLFGA
