SECY_VAULI
ID SECY_VAULI Reviewed; 436 AA.
AC B7T1W7;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465};
OS Vaucheria litorea (Yellow-green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Xanthophyceae;
OC Vaucheriales; Vaucheriaceae; Vaucheria.
OX NCBI_TaxID=109269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2940;
RX PubMed=19004808; DOI=10.1073/pnas.0804968105;
RA Rumpho M.E., Worful J.M., Lee J., Kannan K., Tyler M.S., Bhattacharya D.,
RA Moustafa A., Manhart J.R.;
RT "Horizontal gene transfer of the algal nuclear gene psbO to the
RT photosynthetic sea slug Elysia chlorotica.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:17867-17871(2008).
CC -!- FUNCTION: The central subunit of the protein translocation channel
CC SecYE. Consists of two halves. These two domains form a lateral gate at
CC the front which open onto the bilayer between TMs 2 and 7, and are
CC clamped together by SecE at the back. The channel is closed by both a
CC pore ring composed of hydrophobic SecY resides and a short helix (helix
CC 2A) on the extracellular side of the membrane which forms a plug (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the plastid Sec protein translocase complex,
CC which is composed of at least SecY and SecE. {ECO:0000255|HAMAP-
CC Rule:MF_01465}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01465}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01465}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000255|HAMAP-
CC Rule:MF_01465}.
CC -!- CAUTION: Bioinformatics prediction programs detect only 8 instead of 10
CC transmembrane regions. {ECO:0000305}.
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DR EMBL; EU912438; ACF70933.1; -; Genomic_DNA.
DR RefSeq; YP_002327516.1; NC_011600.1.
DR AlphaFoldDB; B7T1W7; -.
DR GeneID; 7056024; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 PANTHER; PTHR10906; PTHR10906; 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 Chloroplast; Membrane; Plastid; Protein transport; Thylakoid;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..436
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000414218"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
SQ SEQUENCE 436 AA; 49694 MW; 64494E122CD4F5EB CRC64;
MNTKLQDSKS PRLKNRILLT ISLLTIVRIG SFIPVPYITK EVLVNLLSAE NSSNNTFAQL
LNTFSGGGNS SFGLLSLGIL PYINASIIIQ LLTTIIPALS KMQKDEGEYG RRKLVDFTRY
LTFFWAIVES ISISYSLREV IFEWNLQVYF LISLSLITGS MIVLWFSELI TKNGLGNGSS
LLICFNIVSN LPDQIKFSLI SLKNQINNFS NIFLLISIFL ITTIGCIYIN EAIIKIPLVS
ARQLLKKTKS EEKNSSNSIL PLRINQAGVM PLVFTSYAIL FFSSLFEIIK KQTNIFNIFF
QYPILNSVIS YWFLKILFWI FYATLIFFFT YFYSTIVLDP KDVAERFRKN SVVILGISPG
SSTRSYLSKI LRFIAKINAI FLIYNIIGLQ ILESILNLNI INIRGLGFTS QLILVNVLID
TIKRIRSFLN EEENYF