##gff-version 3 P0AGA2 UniProtKB Chain 1 443 . . . ID=PRO_0000131721;Note=Protein translocase subunit SecY P0AGA2 UniProtKB Topological domain 1 22 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Transmembrane 23 35 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Topological domain 36 60 . . . Note=Periplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250 P0AGA2 UniProtKB Transmembrane 61 96 . . . Note=Discontinuously helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250 P0AGA2 UniProtKB Intramembrane 61 70 . . . Note=Helical%3B Name%3DHelix 2A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Intramembrane 71 76 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Intramembrane 77 96 . . . Note=Helical%3B Name%3DHelix 2B;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Topological domain 97 115 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Transmembrane 116 131 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Topological domain 132 164 . . . Note=Periplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Transmembrane 165 178 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Topological domain 179 183 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Transmembrane 184 200 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Topological domain 201 223 . . . Note=Periplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Transmembrane 224 237 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Topological domain 238 273 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Transmembrane 274 287 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Topological domain 288 313 . . . Note=Periplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Transmembrane 314 329 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Topological domain 330 380 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Transmembrane 381 395 . . . Note=Helical%3B Name%3D9;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Topological domain 396 396 . . . Note=Periplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Transmembrane 397 413 . . . Note=Helical%3B Name%3D10;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Topological domain 414 443 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0AGA2 UniProtKB Mutagenesis 40 40 . . . Note=In secY100%3B temperature-sensitive. P->S P0AGA2 UniProtKB Mutagenesis 60 74 . . . Note=Some loss of viability%2C supports protein translocation%3B strongly suppresses defective and missing signal sequences%3B transient transmembrane channels open. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17531809,ECO:0000269|PubMed:17531810;Dbxref=PMID:17531809,PMID:17531810 P0AGA2 UniProtKB Mutagenesis 65 70 . . . Note=Grows almost as well as wild-type%2C supports protein translocation%3B strongly suppresses defective and missing signal sequences%3B transient transmembrane channels open. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17531809,ECO:0000269|PubMed:17531810;Dbxref=PMID:17531809,PMID:17531810 P0AGA2 UniProtKB Mutagenesis 67 67 . . . Note=In prlA3%3B altered signal sequence interaction%2C transient channel opening and closing in presence of oxidant%3B massive ion flux when cross-linked to SecEC-120 mutation. F->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17531809;Dbxref=PMID:17531809 P0AGA2 UniProtKB Mutagenesis 167 167 . . . Note=In secY100%3B temperature-sensitive. G->E P0AGA2 UniProtKB Mutagenesis 240 240 . . . Note=In secY24%3B temperature-sensitive at 42 degrees Celsius%2C impairs interaction with SecE even at 30 degrees in vitro. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8183945;Dbxref=PMID:8183945 P0AGA2 UniProtKB Mutagenesis 282 282 . . . Note=In prlA401%3B altered signal sequence interaction%2C transient transmembrane channels open. S->R P0AGA2 UniProtKB Mutagenesis 286 286 . . . Note=In prlA4-1%3B altered signal sequence interaction. F->Y P0AGA2 UniProtKB Mutagenesis 287 287 . . . Note=In secY161%3B altered signal sequence interaction. P->L P0AGA2 UniProtKB Mutagenesis 290 290 . . . Note=In secY121%3B altered signal sequence interaction. I->T P0AGA2 UniProtKB Mutagenesis 357 357 . . . Note=In secY39%3B cold-sensitive. R->H P0AGA2 UniProtKB Mutagenesis 363 363 . . . Note=In secY40%3B cold-sensitive. A->S P0AGA2 UniProtKB Mutagenesis 408 408 . . . Note=In prlA4-2%3B altered signal sequence interaction. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17531809;Dbxref=PMID:17531809 P0AGA2 UniProtKB Mutagenesis 424 443 . . . Note=No longer complements secY24%2C a temperature-sensitive secY mutation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20855604;Dbxref=PMID:20855604 P0AGA2 UniProtKB Helix 17 36 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Beta strand 41 44 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 46 52 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 59 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Turn 66 69 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Turn 71 75 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 83 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 100 106 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 110 138 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 155 176 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Turn 178 181 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Beta strand 182 184 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 186 196 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 200 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Turn 209 213 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 217 239 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Beta strand 242 251 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Beta strand 258 267 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Beta strand 269 272 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 274 290 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Turn 291 294 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 301 309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 315 336 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 339 348 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 360 394 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Beta strand 401 403 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE P0AGA2 UniProtKB Helix 404 426 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5GAE