SECY_NEOYE
ID SECY_NEOYE Reviewed; 411 AA.
AC Q1XDJ1; A0MM94;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465};
OS Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX NCBI_TaxID=2788;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Qingdao;
RA Wang M.Q., Mao Y.X.;
RT "Cloning and analysis of the Porphyra yezoensis gene for secY.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U-51;
RA Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; DQ995187; ABJ91302.1; -; Genomic_DNA.
DR EMBL; AP006715; BAE92420.1; -; Genomic_DNA.
DR RefSeq; YP_536977.1; NC_007932.1.
DR AlphaFoldDB; Q1XDJ1; -.
DR SMR; Q1XDJ1; -.
DR GeneID; 3978774; -.
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_0000277278"
FT TRANSMEM 11..31
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 253..273
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 349..369
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"
FT CONFLICT 121
FT /note="A -> T (in Ref. 1; ABJ91302)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="F -> S (in Ref. 1; ABJ91302)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="I -> T (in Ref. 1; ABJ91302)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 45558 MW; 988DDCD85BFB28C2 CRC64;
MSQKSDLRNR IIFTLFLLVL ARLGIFIPVP GIDHDAFYAS VEKNTLVNFL NIFSGGGFST
IGIFALGIVP YINSSIVMQL LTKIVPNLEK LQKEEGELGR QKITQITRYL ALGWATLQSG
AISIWVKPYV FNWNFAFVCE SVLALTAGSM IIMWLSELIT EKGIGNGASL LIFQNIVSGL
PKNFTQSFFD ASYSNASLKF GLFIAIFLLM IIITICVQEG TRRIKIISAR QLGKSSILDP
NSYLPLKLNQ GGVMPIVFAS ASMALPSYLT QIIQNKTLLQ ILYLFCPNGS LYLLLYCALI
LFFSYFYTSI VMNPEDIAIN LKKMGASIPN IRPGQATIDY LQVILNRLTF LGASFLFTVA
LIPFIIEKVT QIQNLRGLGA TSLLILVGVA IDTAKQIQTY VISKKYDSMT K