##gff-version 3 P0A8M3 UniProtKB Chain 1 642 . . . ID=PRO_0000100973;Note=Threonine--tRNA ligase P0A8M3 UniProtKB Domain 1 61 . . . Note=TGS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01228 P0A8M3 UniProtKB Region 1 224 . . . Note=Correctly edits mischarged seryl-tRNA(Thr);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15525511;Dbxref=PMID:15525511 P0A8M3 UniProtKB Region 1 62 . . . Note=N1 domain;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Region 2 241 . . . Note=N-terminal region which includes the editing domain%2C important for catalytic efficiency%2C its loss increases mischarging with L-serine%2C deacylation of incorrectly charged tRNA no longer occurs%2C partially complements a deletion strain;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Region 63 224 . . . Note=N2 domain%2C the editing domain;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Region 200 219 . . . Note=TRNA acceptor stem binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Region 243 534 . . . Note=Catalytic;Ontology_term=ECO:0000255,ECO:0000305;evidence=ECO:0000255|HAMAP-Rule:MF_00184,ECO:0000305|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Region 535 642 . . . Note=Anticodon recognition;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 246 249 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11953757;Dbxref=PMID:11953757 P0A8M3 UniProtKB Binding site 309 309 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10319817,ECO:0007744|PDB:1QF6;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 313 317 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 325 325 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 334 334 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_00184,ECO:0000269|PubMed:10319817,ECO:0000269|PubMed:10881191,ECO:0000269|PubMed:11136973,ECO:0000269|PubMed:11953757;Dbxref=PMID:10319817,PMID:10881191,PMID:11136973,PMID:11953757 P0A8M3 UniProtKB Binding site 342 349 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11953757;Dbxref=PMID:11953757 P0A8M3 UniProtKB Binding site 348 349 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 363 365 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10319817,ECO:0007744|PDB:1QF6;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 363 363 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 375 375 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 376 376 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10319817,ECO:0007744|PDB:1QF6;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 379 379 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 381 381 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10319817,ECO:0007744|PDB:1QF6;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 385 385 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_00184,ECO:0000269|PubMed:10319817,ECO:0000269|PubMed:10881191,ECO:0000269|PubMed:11136973,ECO:0000269|PubMed:11953757;Dbxref=PMID:10319817,PMID:10881191,PMID:11136973,PMID:11953757 P0A8M3 UniProtKB Binding site 462 462 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 479 480 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10319817,ECO:0007744|PDB:1QF6;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 484 484 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 489 503 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11953757;Dbxref=PMID:11953757 P0A8M3 UniProtKB Binding site 511 511 . . . Ontology_term=ECO:0000255,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_00184,ECO:0000269|PubMed:10319817,ECO:0000269|PubMed:10881191,ECO:0000269|PubMed:11136973;Dbxref=PMID:10319817,PMID:10881191,PMID:11136973 P0A8M3 UniProtKB Binding site 517 517 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10319817,ECO:0007744|PDB:1QF6;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 520 520 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 547 549 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11953757;Dbxref=PMID:11953757 P0A8M3 UniProtKB Binding site 547 549 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 575 586 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11953757;Dbxref=PMID:11953757 P0A8M3 UniProtKB Binding site 575 583 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 589 589 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 595 600 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11953757;Dbxref=PMID:11953757 P0A8M3 UniProtKB Binding site 595 600 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 609 609 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11953757;Dbxref=PMID:11953757 P0A8M3 UniProtKB Binding site 609 609 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Binding site 615 615 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11953757;Dbxref=PMID:11953757 P0A8M3 UniProtKB Modified residue 286 286 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|HAMAP-Rule:MF_00184,ECO:0000269|PubMed:18723842;Dbxref=PMID:18723842 P0A8M3 UniProtKB Mutagenesis 73 77 . . . Note=No longer edits mischarged L-seryl-tRNA(Thr)%2C mischarges tRNA(Thr) with L-serine%2C correct acylation is unaffected. HSCAH->ASCAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11136973;Dbxref=PMID:11136973 P0A8M3 UniProtKB Mutagenesis 156 156 . . . Note=Mischarges tRNA(Thr) with L-serine. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15525511;Dbxref=PMID:15525511 P0A8M3 UniProtKB Mutagenesis 180 180 . . . Note=No longer edits mischarged L-seryl-tRNA(Thr)%2C mischarges tRNA(Thr) with L-serine%2C correct acylation is unaffected. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11136973;Dbxref=PMID:11136973 P0A8M3 UniProtKB Mutagenesis 182 182 . . . Note=Very high mischarging of tRNA(Thr) with L-serine. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15525511;Dbxref=PMID:15525511 P0A8M3 UniProtKB Mutagenesis 186 186 . . . Note=Mischarges tRNA(Thr) with L-serine. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15525511;Dbxref=PMID:15525511 P0A8M3 UniProtKB Mutagenesis 296 296 . . . Note=Confers resistance to borrelidin (BN)%3B KM for L-Thr is unchanged%2C KM for ATP increases to 187 uM%2C KI for BN increases to 4.5 nM. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15507440;Dbxref=PMID:15507440 P0A8M3 UniProtKB Mutagenesis 307 307 . . . Note=KI for BN increases 10-fold%2C no change in aminoacylation activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15507440;Dbxref=PMID:15507440 P0A8M3 UniProtKB Mutagenesis 309 309 . . . Note=10-fold increase in KM for Thr for activation%2C 240-fold decrease in aminoacyl transfer. Cells have a long lag phase and reach stationary phase at a lower cell density. KI for BN increases 1000-fold%2C supports growth in the presence of BN. H->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15507440,ECO:0000269|PubMed:18997014;Dbxref=PMID:15507440,PMID:18997014 P0A8M3 UniProtKB Mutagenesis 334 334 . . . Note=Does not complement a deletion strain. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Mutagenesis 337 337 . . . Note=KI for BN increases 12-fold%2C no change in aminoacylation activity%2C supports growth in the presence of BN. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15507440;Dbxref=PMID:15507440 P0A8M3 UniProtKB Mutagenesis 363 363 . . . Note=700-fold decrease in kcat for Thr activation%2C 1000-fold decrease in kcat of aminoacylation%2C no change in KM. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18997014;Dbxref=PMID:18997014 P0A8M3 UniProtKB Mutagenesis 381 381 . . . Note=100-fold increase in KM for Thr for activation. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18997014;Dbxref=PMID:18997014 P0A8M3 UniProtKB Mutagenesis 385 385 . . . Note=Does not complement a deletion strain. H->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Mutagenesis 465 465 . . . Note=35-fold decrease in kcat for Thr activation%2C 570-fold decrease in kcat of aminoacylation%2C no change in KM. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18997014;Dbxref=PMID:18997014 P0A8M3 UniProtKB Mutagenesis 479 479 . . . Note=Wild-type Thr activation and aminoacylation. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18997014;Dbxref=PMID:18997014 P0A8M3 UniProtKB Mutagenesis 489 489 . . . Note=Confers resistance to borrelidin (BN)%3B KM for L-thr is unchanged%2C KM for ATP increases to 163 uM%2C KI for BN increases to 7.8 nM%2C supports growth in the presence of BN. L->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15507440;Dbxref=PMID:15507440 P0A8M3 UniProtKB Mutagenesis 489 489 . . . Note=KI for BN increases 1500-fold%2C no change in aminoacylation activity%2C supports growth in the presence of BN. L->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15507440;Dbxref=PMID:15507440 P0A8M3 UniProtKB Mutagenesis 511 511 . . . Note=Does not complement a deletion strain%2C has dominant lethal effect in presence of wild-type gene%2C probably due to repression of the wild-type gene. H->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10319817;Dbxref=PMID:10319817 P0A8M3 UniProtKB Mutagenesis 531 531 . . . Note=KI for BN increases 8-fold%2C decreases aminoacylation activity%2C does not support growth in the presence of BN. G->GEGK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15507440;Dbxref=PMID:15507440 P0A8M3 UniProtKB Sequence conflict 195 195 . . . Note=H->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P0A8M3 UniProtKB Beta strand 3 5 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Beta strand 11 13 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Helix 20 27 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Helix 29 34 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Beta strand 37 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Beta strand 43 46 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Beta strand 55 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Helix 65 86 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Beta strand 101 107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Helix 114 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Beta strand 135 138 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Helix 141 150 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Helix 154 163 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Beta strand 171 175 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Beta strand 178 183 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Helix 190 192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Beta strand 196 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Helix 206 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Beta strand 214 222 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1TKE P0A8M3 UniProtKB Helix 226 240 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QF6 P0A8M3 UniProtKB Helix 244 250 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 254 257 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8OU8 P0A8M3 UniProtKB Beta strand 260 266 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8OU8 P0A8M3 UniProtKB Helix 268 287 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 297 300 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 301 306 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 309 312 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 314 316 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 319 322 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 325 329 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 331 333 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1QF6 P0A8M3 UniProtKB Helix 334 341 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 348 350 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 352 362 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 367 369 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Turn 372 374 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 377 388 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 390 392 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 393 409 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Turn 410 412 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 417 421 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 431 447 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 453 455 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 461 463 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HWR P0A8M3 UniProtKB Beta strand 465 471 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 477 488 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 489 492 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 502 505 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVK P0A8M3 UniProtKB Beta strand 508 517 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 518 529 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Turn 535 537 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 542 548 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 549 551 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 552 564 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 569 572 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 574 576 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4P3O P0A8M3 UniProtKB Helix 578 587 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 591 596 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 598 603 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 605 610 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Beta strand 615 620 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL P0A8M3 UniProtKB Helix 621 633 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1EVL