##gff-version 3 P0AEJ4 UniProtKB Chain 1 450 . . . ID=PRO_0000074759;Note=Sensor histidine kinase EnvZ P0AEJ4 UniProtKB Topological domain 1 15 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:2824492;Dbxref=PMID:2824492 P0AEJ4 UniProtKB Transmembrane 16 35 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:2824492;Dbxref=PMID:2824492 P0AEJ4 UniProtKB Topological domain 36 158 . . . Note=Periplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:2824492;Dbxref=PMID:2824492 P0AEJ4 UniProtKB Transmembrane 159 179 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:2824492;Dbxref=PMID:2824492 P0AEJ4 UniProtKB Topological domain 180 450 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305,ECO:0000305,ECO:0000305;evidence=ECO:0000305|PubMed:15919996,ECO:0000305|PubMed:17635923,ECO:0000305|PubMed:2824492;Dbxref=PMID:15919996,PMID:17635923,PMID:2824492 P0AEJ4 UniProtKB Domain 180 232 . . . Note=HAMP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00102 P0AEJ4 UniProtKB Domain 240 440 . . . Note=Histidine kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00107 P0AEJ4 UniProtKB Region 223 289 . . . Note=Cytoplasmic dimerization domain (CDD)%2C when dimerized forms osmosensitive core;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17635923;Dbxref=PMID:17635923 P0AEJ4 UniProtKB Motif 71 75 . . . Note=PolyP-periplasmic motif;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:29953503;Dbxref=PMID:29953503 P0AEJ4 UniProtKB Motif 201 205 . . . Note=PolyP-cytoplasmic motif;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:29953503;Dbxref=PMID:29953503 P0AEJ4 UniProtKB Binding site 243 243 . . . Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:4KP4 P0AEJ4 UniProtKB Binding site 347 351 . . . Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:4KP4 P0AEJ4 UniProtKB Binding site 373 373 . . . Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:4KP4 P0AEJ4 UniProtKB Binding site 392 393 . . . Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:4KP4 P0AEJ4 UniProtKB Binding site 402 406 . . . Ontology_term=ECO:0007744;evidence=ECO:0007744|PDB:4KP4 P0AEJ4 UniProtKB Modified residue 243 243 . . . Note=Phosphohistidine%3B by autocatalysis;Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00107,ECO:0000269|PubMed:8132603;Dbxref=PMID:8132603 P0AEJ4 UniProtKB Mutagenesis 1 38 . . . Note=In envZ115%3B low constitutive expression of OmpC or OmpF at low and high osmolarity. Phosphorylates and dephosphorylates OmpR. MRRLRFSPRSSFARTLLLIVTLLFASLVTTYLVVLNFA->MTMITDSL;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:2558046,ECO:0000269|PubMed:3056929;Dbxref=PMID:2558046,PMID:3056929 P0AEJ4 UniProtKB Mutagenesis 18 18 . . . Note=No OmpC%2C constitutive OmpF%2C with or without sucrose. No change in phosphorylation or dephosphorylation of OmpR. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1323560;Dbxref=PMID:1323560 P0AEJ4 UniProtKB Mutagenesis 41 41 . . . Note=Constitutive OmpC%2C no OmpF%2C with or without sucrose. Phosphorylates but does not dephosphorylate OmpR. P->L%2CS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1323560;Dbxref=PMID:1323560 P0AEJ4 UniProtKB Mutagenesis 73 74 . . . Note=Decreased interaction with MzrA. PP->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29953503;Dbxref=PMID:29953503 P0AEJ4 UniProtKB Mutagenesis 180 180 . . . Note=No OmpC%2C constitutive OmpF%2C with or without sucrose. Weakly phosphorylates OmpR%2C dephosphorylates normally. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1323560;Dbxref=PMID:1323560 P0AEJ4 UniProtKB Mutagenesis 185 185 . . . Note=Constitutive OmpC%2C no OmpF%2C with or without sucrose. Weakly phosphorylates but does not dephosphorylate OmpR. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:1323560;Dbxref=PMID:1323560 P0AEJ4 UniProtKB Mutagenesis 193 193 . . . Note=Promotes the formation of alpha-helical secondary structure of the HAMP domain. A->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17635923;Dbxref=PMID:17635923 P0AEJ4 UniProtKB Mutagenesis 193 193 . . . Note=No effect. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17635923;Dbxref=PMID:17635923 P0AEJ4 UniProtKB Mutagenesis 202 204 . . . Note=Decreased protein homodimerization%2C constitutive OmpC%2C little to no OmpF with or without salt%2C no interaction with MzrA. PPP->AAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29953503;Dbxref=PMID:29953503 P0AEJ4 UniProtKB Mutagenesis 234 234 . . . Note=Autophosphorylation by cytoplasmic dimerization domain (CDD) is resistant to waldiomycin. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27999439;Dbxref=PMID:27999439 P0AEJ4 UniProtKB Mutagenesis 242 242 . . . Note=Autophosphorylation by CDD is resistant to waldiomycin%2C CDD peptide probably no longer binds waldiomycin. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27999439;Dbxref=PMID:27999439 P0AEJ4 UniProtKB Mutagenesis 243 243 . . . Note=Does not autophosphorylate%2C does not dephosphorylate OmpR in vitro%2C no OmpC or OmpF at 0%25 sucrose%2C low levels of OmpC and very low levels of OmpF at 15%25 sucrose. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2277041;Dbxref=PMID:2277041 P0AEJ4 UniProtKB Mutagenesis 243 243 . . . Note=Does not autophosphorylate%2C does not transfer phosphate to OmpR%2C increased expression of ompC%2C decreased expression of OmpF. H->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2668953;Dbxref=PMID:2668953 P0AEJ4 UniProtKB Mutagenesis 244 244 . . . Note=Autophosphorylation by CDD is resistant to waldiomycin%2C CDD peptide probably no longer binds waldiomycin. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27999439;Dbxref=PMID:27999439 P0AEJ4 UniProtKB Mutagenesis 247 247 . . . Note=Autophosphorylation by CDD is somewhat resistant to waldiomycin. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27999439;Dbxref=PMID:27999439 P0AEJ4 UniProtKB Mutagenesis 247 247 . . . Note=In envZ11/MH1461%3B OmpF- OmpC constitutive. Also prevents expression of PhoA and LamB. Phosphorylates OmpR but does not dephosphorylate it. T->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1323560,ECO:0000269|PubMed:2668281,ECO:0000269|PubMed:3536870;Dbxref=PMID:1323560,PMID:2668281,PMID:3536870 P0AEJ4 UniProtKB Mutagenesis 248 248 . . . Note=Autophosphorylation by CDD is resistant to waldiomycin%2C CDD peptide probably no longer binds waldiomycin%2C alters structure. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27999439;Dbxref=PMID:27999439 P0AEJ4 UniProtKB Mutagenesis 347 347 . . . Note=Loss of ATP binding%3B loss of autophosphorylation. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9817206;Dbxref=PMID:9817206 P0AEJ4 UniProtKB Helix 43 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XGA P0AEJ4 UniProtKB Beta strand 60 63 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XGA P0AEJ4 UniProtKB Beta strand 69 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XGA P0AEJ4 UniProtKB Helix 74 84 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XGA P0AEJ4 UniProtKB Beta strand 87 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XGA P0AEJ4 UniProtKB Helix 91 97 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XGA P0AEJ4 UniProtKB Helix 99 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XGA P0AEJ4 UniProtKB Helix 106 116 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XGA P0AEJ4 UniProtKB Beta strand 120 125 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XGA P0AEJ4 UniProtKB Beta strand 132 137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XGA P0AEJ4 UniProtKB Beta strand 143 148 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5XGA P0AEJ4 UniProtKB Helix 229 257 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZCC P0AEJ4 UniProtKB Helix 261 263 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZCC P0AEJ4 UniProtKB Helix 264 287 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3ZCC P0AEJ4 UniProtKB Turn 290 292 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CTI P0AEJ4 UniProtKB Beta strand 297 299 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CTI P0AEJ4 UniProtKB Helix 301 309 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CTI P0AEJ4 UniProtKB Beta strand 314 316 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BXD P0AEJ4 UniProtKB Beta strand 319 322 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CTI P0AEJ4 UniProtKB Beta strand 329 332 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KP4 P0AEJ4 UniProtKB Helix 334 350 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CTI P0AEJ4 UniProtKB Beta strand 352 354 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KP4 P0AEJ4 UniProtKB Beta strand 356 359 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CTI P0AEJ4 UniProtKB Beta strand 369 373 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CTI P0AEJ4 UniProtKB Beta strand 378 380 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CTI P0AEJ4 UniProtKB Helix 383 386 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KP4 P0AEJ4 UniProtKB Helix 394 397 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4KP4 P0AEJ4 UniProtKB Helix 402 415 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CTI P0AEJ4 UniProtKB Beta strand 419 422 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CTI P0AEJ4 UniProtKB Turn 426 428 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1BXD P0AEJ4 UniProtKB Beta strand 431 435 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4CTI