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 | Saci_0574 |
Created Date | 3-June-2014 |
Organism | Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) |
NCBI Taxa ID | 330779 |
Phosphorylation | Position | Peptide | Code | Type | References | 110 | LTTQEGKSKFTQAEK | S | HTP | [1] | |
Reference | [1]Archaeal signal transduction: impact of protein phosphatase deletions on cell size, motility, and energy metabolism in Sulfolobus acidocaldarius. Reimann J,Esser D,Orell A,Amman F,Pham TK,Noirel J,Lindås AC,Bernander R,Wright PC,Siebers B,Albers SV Mol. Cell Proteomics 2013, Dec;12(12):3908-23. [ PMID:24078887] |
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 21 47 Helical; Name=Helix 1; (By similarity) TRANSMEM 61 89 Discontinuously helical; Name=Helix 2 (By similarity) TRANSMEM 111 134 Helical; Name=Helix 3; (By similarity) TRANSMEM 143 167 Helical; Name=Helix 4; (By similarity) TRANSMEM 175 193 Helical; Name=Helix 5; (By similarity) TRANSMEM 237 258 Helical; Name=Helix 6; (By similarity) TRANSMEM 284 305 Helical; Name=Helix 7; (By similarity) TRANSMEM 342 361 Helical; Name=Helix 8; (By similarity) TRANSMEM 405 423 Helical; Name=Helix 9; (By similarity) TRANSMEM 427 441 Helical; Name=Helix 10; (By similarity) |
| Cellmembrane; Completeproteome; Membrane; Proteintransport; Translocation; Transmembrane; Transmembranehelix; Transport |
Protein Sequence | MGFMDFLAKM GENLPAVSKP KDKPTLTRKL LWTFIGLIVY LLMASIPLYG VTSSNSFLSN 60 FLAQQIIFAS SQGTLAQLGI GPVITSGLIM QILVGSKLIN VDLTTQEGKS KFTQAEKALA 120 LIFIIVESSL FGYVFTRATS NILLPIIVVV QLIIASYIIL LLDEMIQKGW GLGSGVSLFI 180 MAGIMKVIFW NMFGIVSVQS QNLPVGFFPL LVSYITSGRN LQEIVLNTSS TTPYQPDLIG 240 LIATVGLTIL IVYLVNTNIY IPVTTQRLRG IRTTVPLNFL YVSSIPVIFV SVLGADIQLF 300 ASLANSISNS ASGILTDIAN AFFFPPQGVP HSVYALVVDP VGAAIYAAVF IVLSIVFGML 360 WIDVAGLDPK TQAEQMIRSG IEIPGMRTNP RIIEGILSKY IYALGFFSSL IVGLIAVVAT 420 FLGTYGTGVG LLLAITIAMQ YYNLLAYERT LEMYPLLKRI VGE 463 |
| GO:0016021 C:integral component of membrane IEA:UniProtKB-KW GO:0005622 C:intracellular IEA:GOC GO:0005886 C:plasma membrane IEA:UniProtKB-SubCell GO:0065002 P:intracellular protein transmembrane transport IEA:UniProtKB-HAMAP GO:0006605 P:protein targeting IEA:UniProtKB-HAMAP |
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