SECY_PORPU
ID SECY_PORPU Reviewed; 411 AA.
AC P51297;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465};
OS Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX NCBI_TaxID=2787;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Avonport;
RA Reith M.E., Munholland J.;
RT "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT genome.";
RL Plant Mol. Biol. Rep. 13:333-335(1995).
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, SecE and SecG. {ECO:0000250}.
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; U38804; AAC08183.1; -; Genomic_DNA.
DR PIR; S73218; S73218.
DR RefSeq; NP_053907.1; NC_000925.1.
DR AlphaFoldDB; P51297; -.
DR SMR; P51297; -.
DR GeneID; 809926; -.
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..411
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131778"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 111..131
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 163..180
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
SQ SEQUENCE 411 AA; 45660 MW; A353DAF0D27863FD CRC64;
MSQKSDLRNR IKFTLLLLVL ARLGIFIPVP GIDHDAFYAS VEKNTLVNFL NIFSGGGFST
IGIFALGIVP YINSSIVMQL LTKIIPDLEK LQKEEGELGR QKITQITRYL ALGWATLQSG
AISIWVKPYV FNWNFTFVCE SVLALTAGSM IIMWLSELIT EKGIGNGASL LIFQNIVSGL
PKNFTQSFFD ANYSNTSIKF GLFIVIFLLM IIITIFVQEG TRRIKIISAR QLGKSSILDP
NSYLPLKLNQ GGVMPIVFAS ASMALPAYLT QLTQNTFLLQ VLYLFCPNGS LYLVLYSVLI
LFFSYFYTSI VMNPEDIATN LKKMGASIPN IRPGQATIDY LQVILNRLTF LGATFLFTVA
LIPFIIEKVA QIQNLRGLGA TSLLILVGVA IDTAKQIQTY VISKKYDSMT K