Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein translocase subunit SecY |
Protein Synonyms/Alias | |
Gene Name | secY |
Gene Synonyms/Alias | SYNPCC7002_A1047 |
Created Date | 3-June-2014 |
Organism | Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum) |
NCBI Taxa ID | 32049 |
Phosphorylation | Position | Peptide | Code | Type | References | 263 | KLYRERTSYLPLRLN | S | HTP | [1] | 262 | RKLYRERTSYLPLRL | T | HTP | [1] | |
Reference | [1]Global phosphoproteomic analysis reveals diverse functions of serine/threonine/tyrosine phosphorylation in the model cyanobacterium Synechococcus sp. strain PCC 7002. Yang MK,Qiao ZX,Zhang WY,Xiong Q,Zhang J,Li T,Ge F,Zhao JD J. Proteome Res. 2013, Apr, 5;12(4):1909-23. [ PMID:23461524] |
Functional Description From UniProt | FUNCTION: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (By similarity) |
| TRANSMEM 29 49 Helical; (By similarity) TRANSMEM 69 89 Helical; (By similarity) TRANSMEM 123 143 Helical; (By similarity) TRANSMEM 153 173 Helical; (By similarity) TRANSMEM 182 202 Helical; (By similarity) TRANSMEM 216 236 Helical; (By similarity) TRANSMEM 274 294 Helical; (By similarity) TRANSMEM 319 339 Helical; (By similarity) TRANSMEM 375 395 Helical; (By similarity) TRANSMEM 398 418 Helical; (By similarity) |
| Cellinnermembrane; Cellmembrane; Completeproteome; Membrane; Proteintransport; Thylakoid; Translocation; Transmembrane; Transmembranehelix; Transport |
Protein Sequence | MVVSREKTPT AQETFMQMAQ AAGLRGRLLV TLGLLVLVRF GVFIPIPGID RVALSEGIQN 60 SPLLGFLDVF AGGGLSAVGI FALGILPYIN ASIIMQLMTA AIPALEDMQK NDGEAGRRKI 120 SQIIRYVTVG WAALQSFGIT LQILRPYALD PGFTFVLETT LALTAGSVFV MWISELITEK 180 GLGNGASLLI FVNIVAVLPR TLGNTIEFAQ TGGRAVIAKV ILLLVVFLIM IVGIVFVQEG 240 TRRIPIVSAR RQVGRKLYRE RTSYLPLRLN QGGVMPIIFA SAVLVLPSSL AGLAGSGEGF 300 FGQAIATIST LLQPGRIPYV LVYLALILFF SYFYASLIVN PVDMAQNLKK MGSSIPGIRP 360 GRATSEYLEK VINRLTLLGA IFLGLVATVP TFVEGATGVT TLRGFGATSL LILVGVAIDT 420 AKQIQTYVIS QRYEGMVKQ 439 |
| GO:0016021 C:integral component of membrane IEA:UniProtKB-KW GO:0005886 C:plasma membrane IEA:UniProtKB-SubCell GO:0042651 C:thylakoid membrane IEA:UniProtKB-SubCell GO:0065002 P:intracellular protein transmembrane transport IEA:UniProtKB-HAMAP GO:0006605 P:protein targeting IEA:UniProtKB-HAMAP GO:0043952 P:protein transport by the Sec complex IEA:UniProtKB-HAMAP |
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