SECY_HALSA
ID SECY_HALSA Reviewed; 491 AA.
AC Q9HPB1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
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=VNG_1719G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AE004437; AAG19959.1; -; Genomic_DNA.
DR PIR; C84324; C84324.
DR RefSeq; WP_010903257.1; NC_002607.1.
DR AlphaFoldDB; Q9HPB1; -.
DR SMR; Q9HPB1; -.
DR STRING; 64091.VNG_1719G; -.
DR PaxDb; Q9HPB1; -.
DR EnsemblBacteria; AAG19959; AAG19959; VNG_1719G.
DR GeneID; 5954217; -.
DR KEGG; hal:VNG_1719G; -.
DR PATRIC; fig|64091.14.peg.1311; -.
DR HOGENOM; CLU_031763_3_0_2; -.
DR InParanoid; Q9HPB1; -.
DR OMA; KWGIGSG; -.
DR OrthoDB; 13531at2157; -.
DR PhylomeDB; Q9HPB1; -.
DR Proteomes; UP000000554; 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:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
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..491
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131762"
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..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..152
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 153..177
FT /note="Helical; Name=Helix 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 178..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 184..202
FT /note="Helical; Name=Helix 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 203..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..365
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 366..385
FT /note="Helical; Name=Helix 8"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 386..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 429..447
FT /note="Helical; Name=Helix 9"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 448..452
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 453..467
FT /note="Helical; Name=Helix 10"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 468..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 491 AA; 52819 MW; 2A89EDFB0015CD6C CRC64;
MGWKEAAAPV LTRMPAVERP EGHVPFRRKM YWTGGVLVLY FFLTNVPLWG IQTAGNDFFG
QFRSLLAGGQ GTVLQLGIGP IVTASIVLQL LGGANLLGLD TDNDPRDQAI YQGLQKFLVG
VMVVLTGAPM VFLGNFLQPS QQLAQSMPGG AFGVEVLIFA QIAAGGILLL FMDEVISKWG
VGSGIGLFIV AGVSQSLVGG LVFWEGGVGS QGLLPTWFDI IVGNVSNMPP LLSGSGIEFL
LMQAGILGLL TTLFIYVVVV YAESVRVEIP LSHARVKGAR GRFPVKLIYA SVLPMILVRA
LQANIQFLGQ ILNSTLASMP TWLGVYGGNG QVTGGLFYYL APIYSPNAWM WWTSGATAAR
WQVLIRIAID LSFMIIGGAI FAIFWVETAD MGPDATARQI QNSGMQIPGF RKNQGVIEKV
MERYIPQVTV IGGALVGLLA VMANMLGTIG NVSGTGLLLT ISITYKLYEE IAEEQMMEMH
PMMREMFGGG D
