SECY_HALMA
ID SECY_HALMA Reviewed; 487 AA.
AC P28542; Q5V1U5;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 25-MAY-2022, entry version 124.
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=rrnAC1589;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1543743; DOI=10.1016/0167-4781(92)90474-e;
RA Arndt E.;
RT "The genes for ribosomal protein L15 and the protein equivalent to secY in
RT the archaebacterium Haloarcula (Halobacterium) marismortui.";
RL Biochim. Biophys. Acta 1130:113-116(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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; X63127; CAA44838.1; -; Genomic_DNA.
DR EMBL; AY596297; AAV46507.1; -; Genomic_DNA.
DR PIR; S22350; S22350.
DR RefSeq; WP_011223736.1; NZ_CP039138.1.
DR AlphaFoldDB; P28542; -.
DR SMR; P28542; -.
DR STRING; 272569.rrnAC1589; -.
DR TCDB; 3.A.5.7.1; the general secretory pathway (sec) family.
DR EnsemblBacteria; AAV46507; AAV46507; rrnAC1589.
DR GeneID; 40152554; -.
DR KEGG; hma:rrnAC1589; -.
DR PATRIC; fig|272569.17.peg.2278; -.
DR eggNOG; arCOG04169; Archaea.
DR HOGENOM; CLU_031763_3_0_2; -.
DR OMA; KWGIGSG; -.
DR Proteomes; UP000001169; Chromosome I.
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..487
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131761"
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..451
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 452..466
FT /note="Helical; Name=Helix 10"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TOPO_DOM 467..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CONFLICT 195
FT /note="S -> T (in Ref. 1; CAA44838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 52533 MW; D8ED3D7179F62ED2 CRC64;
MSWKDTAEPL LVRMPAVQRP EGHVPFKRKL TWTGGVLLLY FFLTNVKLFG LDIDASQQVF
GRFSSILASG QGSIMQLGIG PIVTASIVLQ LLGGADLLGL NTQDDPRDQI LYQGLQKLLV
LVMICLTGLP MVFAGGFLPA DTAVANSLGI GTAGVQWLIF AQMFVGGVLI LFMDEVISKW
GVGSGIGLFI VAGVSQRLVG GLLTAPFLGN SEGIIYTWYL FITGERGTGP VLAADGLQTV
LLQGELLGLF TTVLIFAVVV YAESVRVEIP LSNARVKGAR GRFPVKLIYA SVLPMILVRA
LQANIQFLGR ILNAQLGSMP AFLGTYANGQ PTGGLFYFLA PIQSRGDWMW WLEGTAQPVW
QILTRVGIDL FVMLVGGAVF AVFWVETTDM GPEATAKQIH NSGMQIPGFR QNVGVIEKVL
ERYIPQVTVI GGALVGLLAV MANMLGTIGG VSGTGLLLTV SITYKLYEEI AEEQLMEMHP
MMRQMFG
