ID   SECY_CYACA              Reviewed;         410 AA.
AC   P46249; Q9MD55;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN   Name=secY {ECO:0000255|HAMAP-Rule:MF_01465};
OS   Cyanidium caldarium (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX   NCBI_TaxID=2771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=RK-1;
RX   PubMed=8980520; DOI=10.1007/bf00020209;
RA   Vogel H., Fischer S., Valentin K.-U.;
RT   "A model for the evolution of the plastid sec apparatus inferred from secY
RT   gene phylogeny.";
RL   Plant Mol. Biol. 32:685-692(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK-1;
RX   PubMed=11040290; DOI=10.1007/s002390010101;
RA   Gloeckner G., Rosenthal A., Valentin K.-U.;
RT   "The structure and gene repertoire of an ancient red algal plastid
RT   genome.";
RL   J. Mol. Evol. 51:382-390(2000).
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   -!- INDUCTION: A monocistronic transcript. {ECO:0000269|PubMed:8980520}.
CC   -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000255|HAMAP-
CC       Rule:MF_01465}.
CC   -!- CAUTION: Bioinformatics prediction programs detect only 9 instead of 10
CC       transmembrane regions. {ECO:0000305}.
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DR   EMBL; AF022186; AAF12924.1; -; Genomic_DNA.
DR   PIR; S47440; S47440.
DR   RefSeq; NP_045170.1; NC_001840.1.
DR   AlphaFoldDB; P46249; -.
DR   SMR; P46249; -.
DR   TCDB; 3.A.5.5.1; the general secretory pathway (sec) family.
DR   GeneID; 800285; -.
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   2: Evidence at transcript level;
KW   Chloroplast; Membrane; Plastid; Protein transport; Thylakoid;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..410
FT                   /note="Protein translocase subunit SecY"
FT                   /id="PRO_0000131773"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        248..268
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        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT   CONFLICT        149
FT                   /note="Missing (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   410 AA;  46243 MW;  7CB0130175B1DF03 CRC64;
     MRPENNLRLR LFQTMKFIAL ERLGLFVPIP GIDQKLFSSD YSNNAISNLL NVFDNNQAPK
     LSVFALGIIP YINATITIQI LSSAFPALKK LQSEEGEIGK KKLNKITKYL SFCFAFIESL
     AIVLRLQKYA FDWNLYFIVQ TTLILISGAM LVMWLADNIS YKGIGTGASV IIFVNIASAF
     AKFLLNQLFV HSIKFLDFAS YFALIVFSIA CIVFVQEAIR KVPIISAKQL DSTSFYSNDY
     FLPLRINQGG VMPIILASSL LALVDYVIRY GLSTLQAVYF INDILPFKIL FLLLYSAFII
     FFNYLYCSLV LNCFELSNNL KKASVVIPSI RPGKMTEKFF KDTLDNLTLF GSGFLAFIVL
     APNFLEFVFH IRVFKGLAVS SLLIVVGVAI DLIKQSKTYV IAKNYENMVH