SECY_HALVD
ID SECY_HALVD Reviewed; 489 AA.
AC Q977V3; D4GTX3; Q8X258;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 25-MAY-2022, entry version 98.
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}; Synonyms=sec61a1;
GN OrderedLocusNames=HVO_2541;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Pohlschroder M.;
RT "The Haloferax volcanii SecY protein.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DS2 / WR 341;
RX PubMed=12579382; DOI=10.1007/s00792-002-0297-0;
RA Irihimovitch V., Ring G., Elkayam T., Konrad Z., Eichler J.;
RT "Isolation of fusion proteins containing SecY and SecE, components of the
RT protein translocation complex from the halophilic archaeon Haloferax
RT volcanii.";
RL Extremophiles 7:71-77(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(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 {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; AF395886; AAK95514.1; -; Genomic_DNA.
DR EMBL; AF336343; AAL73212.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE03186.1; -; Genomic_DNA.
DR RefSeq; WP_004042558.1; NC_013967.1.
DR AlphaFoldDB; Q977V3; -.
DR SMR; Q977V3; -.
DR STRING; 309800.C498_07995; -.
DR EnsemblBacteria; ADE03186; ADE03186; HVO_2541.
DR GeneID; 8925650; -.
DR KEGG; hvo:HVO_2541; -.
DR eggNOG; arCOG04169; Archaea.
DR HOGENOM; CLU_031763_3_0_2; -.
DR OMA; KWGIGSG; -.
DR OrthoDB; 13531at2157; -.
DR Proteomes; UP000008243; 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; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..489
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131763"
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..110
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 111..135
FT /note="Helical; Name=Helix 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 136..153
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 154..178
FT /note="Helical; Name=Helix 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 179..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 185..203
FT /note="Helical; Name=Helix 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 204..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..364
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 365..384
FT /note="Helical; Name=Helix 8"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 385..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 428..446
FT /note="Helical; Name=Helix 9"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 447..450
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 451..465
FT /note="Helical; Name=Helix 10"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 466..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CONFLICT 451
FT /note="Missing (in Ref. 1; AAK95514)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 52325 MW; E3F0EFDEDD6AC4FF CRC64;
MGWKDAAEPV LSRMPAVARP EGHVPFRRKL GWTGGILVLY FFLTNVTLFG LDAATANDLF
GQFRSILAGQ QGSVLQLGIG PIVTASIVLQ LLGGADLLGL DTDNNPRDQV LYQGLQKLLV
GVMICLTGLP MVFAGNFLPA DQAVATSLGI GTVGVKGLIF AQIAVGGVLI LFMDEIVSKW
GVGSGVGLFI IAGVSQQLVG GLFSWQGLGG TSGFFATWIG IITGAIELPA SPTDLLSTVF
LGQGQLLALI TTLLIFGIVV YAESVRVEIP LSHARVKGAR GRFPVKLIYA SVLPMILVRA
LQANIQFLGR FLNSSWVGMP AWLGQYTSGQ VTGGLLYYLA PIQSRSDWMW FLGLTSADPL
DIAIRVLIDL IFMIVGGAVF AIFWVETTGM GPKSTAQQIQ NSGMQIPGFR RNPQVIERVM
ERYIPQVTVI GGALVGLLAV MANMLGTIGA VSGTGLLLTV SITYKLYEEI AEEQLMEMHP
MMRNMFGSE
