SECY_HETA2
ID SECY_HETA2 Reviewed; 454 AA.
AC B2XTD8;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465};
GN OrderedLocusNames=Heak293_Cp129;
OS Heterosigma akashiwo (strain NIES-293 / 8280G21-1).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Raphidophyceae; Chattonellales;
OC Chattonellaceae; Heterosigma.
OX NCBI_TaxID=536047;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18462506; DOI=10.1186/1471-2164-9-211;
RA Cattolico R.A., Jacobs M.A., Zhou Y., Chang J., Duplessis M., Lybrand T.,
RA McKay J., Ong H.C., Sims E., Rocap G.;
RT "Chloroplast genome sequencing analysis of Heterosigma akashiwo CCMP452
RT (West Atlantic) and NIES293 (West Pacific) strains.";
RL BMC Genomics 9:211-211(2008).
CC -!- FUNCTION: The central subunit of the protein translocation channel
CC SecYE. 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. {ECO:0000255|HAMAP-Rule:MF_01465}.
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}.
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DR EMBL; EU168190; ABV66036.1; -; Genomic_DNA.
DR RefSeq; YP_001936430.1; NC_010772.1.
DR AlphaFoldDB; B2XTD8; -.
DR SMR; B2XTD8; -.
DR GeneID; 6335582; -.
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; 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.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; Plastid; Protein transport; Thylakoid;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..454
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000414217"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
SQ SEQUENCE 454 AA; 50963 MW; C14BDA0092BCDD56 CRC64;
MTLEKNKDSF TNIIDLSLIN KEQKVTFTPT KEIYTELLKK RLLTIALLVF IIKIGMAIPL
PYIDQTKLLN NATSMFDLSG PGLAAVSARA SQKIGLFTLG ITPSINASII LQLAFVINPN
LKKLQREEGE SGRRKLIKYT RYLTLLLAIT QSVFLIFSLR AFIFEWSILK LFELSCVLSS
GAMIILWISE CITKTGITNG SSFLIFLNIV SVLPEQIGMS FKNLDIFSFE GLIVILTFSI
TVWAAIFLQQ TLYIIPLKNP KLGQNELTKK LVEDSLYLPF RLNQAGVMPV VFASYLIPIL
KTGGIYILLK INSFNLFPFL IKFPEVVNQS LESIVEAGLI CLFALFYSGL IIDPKDVADE
LQKSGFFIFA IRPGEKTRNY LEKIFKELSL IGALILAFNV VLLNLVGFVF NLSIFKGFSI
GSQIILLGVV TEILQKVQAL VLNDVYKRIR DRNK