SECY_AERPE
ID SECY_AERPE Reviewed; 457 AA.
AC Q9YDD0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 25-MAY-2022, entry version 107.
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=APE_0983.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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; BA000002; BAA79967.2; -; Genomic_DNA.
DR PIR; G72695; G72695.
DR AlphaFoldDB; Q9YDD0; -.
DR SMR; Q9YDD0; -.
DR STRING; 272557.APE_0983.1; -.
DR EnsemblBacteria; BAA79967; BAA79967; APE_0983.1.
DR KEGG; ape:APE_0983.1; -.
DR PATRIC; fig|272557.25.peg.711; -.
DR eggNOG; arCOG04169; Archaea.
DR Proteomes; UP000002518; 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.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..457
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131759"
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..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..146
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 147..171
FT /note="Helical; Name=Helix 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 172..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 179..197
FT /note="Helical; Name=Helix 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 198..229
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 230..251
FT /note="Helical; Name=Helix 6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 252..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 277..298
FT /note="Helical; Name=Helix 7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 299..332
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 333..352
FT /note="Helical; Name=Helix 8"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 353..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 396..414
FT /note="Helical; Name=Helix 9"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 415..417
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 418..432
FT /note="Helical; Name=Helix 10"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 433..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 457 AA; 49901 MW; 8B93F4F2AAA58CA7 CRC64;
MGVIDVLAAV GERFPAVRKP ERKPTLYRRL AWTGVILVLY FIMSNIPLYG IPPQNIGGQV
DLQRIIFASS AGTLMELGIG PIVTASLIIQ VLVGAKIIKL DLADPEGRRK FTSAQKVLAL
AFAALEAVAF TVGGRYWVGT AIEPGPLDYA LVSLQLFLGA LLVIYFDEVM QKGWGIGSAI
SLFILAGVAQ GVVWSIFGTI PGVAQDYGLV PAIISNPDLT LLARPNGFPD LTGFFTTLAA
IILLVYLQAM RVEIPITSER FKGIRSRVPL QFIYVTNIPI LLVGILVSDL LLVQRLLADY
LGVESRAYQI YSSIVYYLSP PRGVVQSIAD PVKTAVFIAS WTVLSIVFGY MWVEIAGLNP
REQAERLIKG GLAIPGMRSD PRVLERVLRR YIYPLTFLSS LIVAALVIVA DIFGAYGTGT
GLLLAVGIIN QYYAMITRER ALETYPLLRR ILGEEVV
