##gff-version 3 Q9I6V6 UniProtKB Chain 1 679 . . . ID=PRO_0000454748;Note=Methyl-accepting chemotaxis protein McpB Q9I6V6 UniProtKB Domain 171 213 . . . Note=PAS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00140 Q9I6V6 UniProtKB Domain 333 385 . . . Note=HAMP 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00102 Q9I6V6 UniProtKB Domain 390 619 . . . Note=Methyl-accepting transducer;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00284 Q9I6V6 UniProtKB Region 8 56 . . . Note=Divergent domain HAMP 1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20399181;Dbxref=PMID:20399181 Q9I6V6 UniProtKB Region 63 112 . . . Note=Divergent domain HAMP 2;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20399181;Dbxref=PMID:20399181 Q9I6V6 UniProtKB Region 111 156 . . . Note=Divergent domain HAMP 3;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:20399181;Dbxref=PMID:20399181 Q9I6V6 UniProtKB Region 289 332 . . . Note=Divergent domain HAMP 4;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:21255112;Dbxref=PMID:21255112 Q9I6V6 UniProtKB Region 405 425 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9I6V6 UniProtKB Region 644 679 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9I6V6 UniProtKB Motif 285 287 . . . Note=DxT. Important for signal propagation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34383467;Dbxref=PMID:34383467 Q9I6V6 UniProtKB Motif 675 679 . . . Note=GWEEF pentapeptide. Important for methylation by CheR2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24714571;Dbxref=PMID:24714571 Q9I6V6 UniProtKB Binding site 234 234 . . . Note=Axial binding residue;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:22622145,ECO:0000269|PubMed:23274111,ECO:0007744|PDB:3VOL,ECO:0007744|PDB:4HI4;Dbxref=PMID:22622145,PMID:23274111 Q9I6V6 UniProtKB Site 264 264 . . . Note=Important for gas binding and signaling;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Site 283 283 . . . Note=Plays a crucial role in stabilization of the heme-bound O(2);Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22622145,ECO:0000269|PubMed:28167524;Dbxref=PMID:22622145,PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 1 56 . . . Note=Unresponsive to O(2). Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21255112;Dbxref=PMID:21255112 Q9I6V6 UniProtKB Mutagenesis 1 37 . . . Note=Behaves like wild-type in a temporal O(2) assay%2C except that it generates a slightly lower tumbling bias at higher O(2) concentration. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21255112;Dbxref=PMID:21255112 Q9I6V6 UniProtKB Mutagenesis 178 178 . . . Note=Mediates wild-type responses to both O(2) and CO. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 179 179 . . . Note=Signal-off mutant that does not respond to either O(2) or CO. L->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34383467;Dbxref=PMID:34383467 Q9I6V6 UniProtKB Mutagenesis 187 187 . . . Note=Signal-off mutant that does not respond to either O(2) or CO. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 190 190 . . . Note=Signal-off mutant that does not respond to either O(2) or CO. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 195 195 . . . Note=Signal-off mutant that does not respond to either O(2) or CO. I->A%2CC;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28167524,ECO:0000269|PubMed:34383467;Dbxref=PMID:28167524,PMID:34383467 Q9I6V6 UniProtKB Mutagenesis 197 197 . . . Note=Signal-off mutant that does not respond to either O(2) or CO. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 199 199 . . . Note=Signal-off mutant that does not respond to either O(2) or CO. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 202 202 . . . Note=Signal-off mutant that does not respond to either O(2) or CO. V->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34383467;Dbxref=PMID:34383467 Q9I6V6 UniProtKB Mutagenesis 213 213 . . . Note=Signal-off mutant that does not respond to either O(2) or CO. I->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:34383467;Dbxref=PMID:34383467 Q9I6V6 UniProtKB Mutagenesis 220 220 . . . Note=Signal-off mutant that does not respond to either O(2) or CO. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 231 231 . . . Note=Mediates wild-type responses to both O(2) and CO. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 233 233 . . . Note=Signal-off mutant that does not respond to either O(2) or CO. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 234 234 . . . Note=Retains 20%25 of heme content. Retains 6%25 of heme content%3B when associated with A-239. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 237 237 . . . Note=Mediates wild-type responses to both O(2) and CO. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 239 239 . . . Note=Mediates wild-type responses to both O(2) and CO. Retains wild-type heme content. Retains 6%25 of heme content%3B when associated with A-234. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 240 240 . . . Note=Mediates wild-type responses to both O(2) and CO. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 251 251 . . . Note=Accelerates autoxidation. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22622145;Dbxref=PMID:22622145 Q9I6V6 UniProtKB Mutagenesis 264 264 . . . Note=Locked signal-on%2C causing cells to tumble constantly in air and in N(2). L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 264 264 . . . Note=Signal-off receptor that does not respond to the addition or removal of O(2). L->D%2CG%2CN%2CP%2CR%2CS%2CW;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 264 264 . . . Note=Shows a reduced tumble response to O(2). Responds to CO. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 264 264 . . . Note=Shows wild-type O(2) responses. L->I%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 264 264 . . . Note=Signal-off mutant that does not respond to the addition or removal of O(2). Does not bind either O(2) or CO. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 264 264 . . . Note=Mediates an O(2) response but exhibits a 30-sec-delayed smooth-swimming response in N(2) and does not respond to CO. L->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 278 278 . . . Note=Signal-off mutant that does not respond to either O(2) or CO. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 283 283 . . . Note=Signal-off mutant that does not respond to the addition or removal of O(2). W->A%2CC%2CG%2CH%2CK%2CP%2CQ%2CR%2CS%2CT%2CY;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 283 283 . . . Note=Signal-on-biased mutant. 50 to 80%25 of the cells continue to tumble when air is removed. Can still bind O(2) in vitro. W->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 283 283 . . . Note=Inverted phenotype. Cannot form stable O(2) bound in vitro. Responds to CO. W->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 283 283 . . . Note=Cannot form stable O(2) bound in vitro. Signal-on-biased mutant. 50 to 80%25 of the cells continue to tumble when air is removed. W->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22622145,ECO:0000269|PubMed:28167524;Dbxref=PMID:22622145,PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 283 283 . . . Note=Does not respond to the addition or removal of O(2). Responds to CO. W->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 285 285 . . . Note=Signal-off mutant that does not respond to either O(2) or CO. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28167524;Dbxref=PMID:28167524 Q9I6V6 UniProtKB Mutagenesis 289 379 . . . Note=Kinase-on mutant that is unresponsive to changes in O(2) concentrations. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21255112;Dbxref=PMID:21255112 Q9I6V6 UniProtKB Mutagenesis 675 679 . . . Note=Abolishes interaction with CheR2 and methylation. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24714571;Dbxref=PMID:24714571 Q9I6V6 UniProtKB Helix 8 26 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4I3M Q9I6V6 UniProtKB Helix 39 41 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4I3M Q9I6V6 UniProtKB Helix 42 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4I3M Q9I6V6 UniProtKB Helix 90 92 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4I3M Q9I6V6 UniProtKB Helix 95 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4I3M Q9I6V6 UniProtKB Helix 139 141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4I3M Q9I6V6 UniProtKB Helix 142 155 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4I3M Q9I6V6 UniProtKB Helix 174 179 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HI4 Q9I6V6 UniProtKB Beta strand 182 190 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HI4 Q9I6V6 UniProtKB Beta strand 194 198 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HI4 Q9I6V6 UniProtKB Helix 200 208 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HI4 Q9I6V6 UniProtKB Helix 210 216 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HI4 Q9I6V6 UniProtKB Helix 222 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HI4 Q9I6V6 UniProtKB Helix 230 233 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HI4 Q9I6V6 UniProtKB Beta strand 234 236 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3VOL Q9I6V6 UniProtKB Helix 237 246 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HI4 Q9I6V6 UniProtKB Beta strand 251 257 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HI4 Q9I6V6 UniProtKB Beta strand 260 270 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HI4 Q9I6V6 UniProtKB Beta strand 276 285 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4HI4 Q9I6V6 UniProtKB Helix 287 304 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3VOL