MCPB_PSEAE
ID MCPB_PSEAE Reviewed; 679 AA.
AC Q9I6V6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Methyl-accepting chemotaxis protein McpB {ECO:0000305};
DE AltName: Full=Aerotaxis transducer Aer2 {ECO:0000305};
GN Name=mcpB {ECO:0000303|PubMed:12142407};
GN Synonyms=aer-2 {ECO:0000303|PubMed:14987771},
GN aer2 {ECO:0000303|PubMed:20399181}, tlpG {ECO:0000303|PubMed:14987771};
GN OrderedLocusNames=PA0176 {ECO:0000312|EMBL:AAG03566.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION IN CHEMOTAXIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12142407; DOI=10.1128/jb.184.16.4374-4383.2002;
RA Ferrandez A., Hawkins A.C., Summerfield D.T., Harwood C.S.;
RT "Cluster II che genes from Pseudomonas aeruginosa are required for an
RT optimal chemotactic response.";
RL J. Bacteriol. 184:4374-4383(2002).
RN [3]
RP FUNCTION IN AEROTAXIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=14987771; DOI=10.1016/s0378-1097(04)00009-6;
RA Hong C.S., Shitashiro M., Kuroda A., Ikeda T., Takiguchi N., Ohtake H.,
RA Kato J.;
RT "Chemotaxis proteins and transducers for aerotaxis in Pseudomonas
RT aeruginosa.";
RL FEMS Microbiol. Lett. 231:247-252(2004).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=15687221; DOI=10.1128/jb.187.4.1533-1535.2005;
RA Hong C.S., Kuroda A., Takiguchi N., Ohtake H., Kato J.;
RT "Expression of Pseudomonas aeruginosa aer-2, one of two aerotaxis
RT transducer genes, is controlled by RpoS.";
RL J. Bacteriol. 187:1533-1535(2005).
RN [5]
RP FUNCTION, SUBUNIT, DOMAIN, METHYLATION, AND MUTAGENESIS OF 1-MET--ARG-56;
RP 1-MET--PRO-37 AND 289-GLU--SER-379.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=21255112; DOI=10.1111/j.1365-2958.2010.07477.x;
RA Watts K.J., Taylor B.L., Johnson M.S.;
RT "PAS/poly-HAMP signalling in Aer-2, a soluble haem-based sensor.";
RL Mol. Microbiol. 79:686-699(2011).
RN [6]
RP INTERACTION WITH CHER2, METHYLATION BY CHER2, AND MUTAGENESIS OF
RP 675-GLY--PHE-679.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=24714571; DOI=10.1126/scisignal.2004849;
RA Garcia-Fontana C., Corral Lugo A., Krell T.;
RT "Specificity of the CheR2 methyltransferase in Pseudomonas aeruginosa is
RT directed by a C-terminal pentapeptide in the McpB chemoreceptor.";
RL Sci. Signal. 7:ra34-ra34(2014).
RN [7]
RP FUNCTION, HEME-BINDING, DOMAIN, AND MUTAGENESIS OF ALA-178; MET-187;
RP ASP-190; ILE-195; TYR-197; ASN-199; PHE-220; ASP-231; PHE-233; HIS-234;
RP PRO-237; HIS-239; GLN-240; LEU-264; GLY-278; TRP-283 AND ASP-285.
RX PubMed=28167524; DOI=10.1128/jb.00003-17;
RA Garcia D., Orillard E., Johnson M.S., Watts K.J.;
RT "Gas sensing and signaling in the PAS-heme domain of the Pseudomonas
RT aeruginosa Aer2 receptor.";
RL J. Bacteriol. 199:0-0(2017).
RN [8]
RP FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=31511598; DOI=10.1038/s41598-019-49697-7;
RA Garcia-Fontana C., Vilchez J.I., Gonzalez-Requena M., Gonzalez-Lopez J.,
RA Krell T., Matilla M.A., Manzanera M.;
RT "The involvement of McpB chemoreceptor from Pseudomonas aeruginosa PAO1 in
RT virulence.";
RL Sci. Rep. 9:13166-13166(2019).
RN [9]
RP INTERACTION WITH CHEB2.
RX PubMed=33187094; DOI=10.3390/ijms21228459;
RA Velando F., Gavira J.A., Rico-Jimenez M., Matilla M.A., Krell T.;
RT "Evidence for pentapeptide-dependent and independent CheB
RT methylesterases.";
RL Int. J. Mol. Sci. 21:0-0(2020).
RN [10]
RP FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF LEU-179; ILE-195; VAL-202 AND
RP ILE-213.
RX PubMed=34383467; DOI=10.1021/acs.biochem.1c00452;
RA Orillard E., Anaya S., Johnson M.S., Watts K.J.;
RT "Oxygen-induced conformational changes in the PAS-heme domain of the
RT Pseudomonas aeruginosa Aer2 receptor.";
RL Biochemistry 60:2610-2622(2021).
RN [11] {ECO:0007744|PDB:3LNR}
RP X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 1-172, AND DOMAIN.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=20399181; DOI=10.1016/j.str.2010.01.013;
RA Airola M.V., Watts K.J., Bilwes A.M., Crane B.R.;
RT "Structure of concatenated HAMP domains provides a mechanism for signal
RT transduction.";
RL Structure 18:436-448(2010).
RN [12] {ECO:0007744|PDB:3VOL}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 173-384 IN COMPLEX WITH HEME,
RP FUNCTION, AND MUTAGENESIS OF HIS-251 AND TRP-283.
RX PubMed=22622145; DOI=10.1039/c2cc32549g;
RA Sawai H., Sugimoto H., Shiro Y., Ishikawa H., Mizutani Y., Aono S.;
RT "Structural basis for oxygen sensing and signal transduction of the heme-
RT based sensor protein Aer2 from Pseudomonas aeruginosa.";
RL Chem. Commun. (Camb.) 48:6523-6525(2012).
RN [13] {ECO:0007744|PDB:4HI4}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 174-289 IN COMPLEX WITH HEME,
RP SUBUNIT, AND DOMAIN.
RX PubMed=23274111; DOI=10.1016/j.jmb.2012.12.011;
RA Airola M.V., Huh D., Sukomon N., Widom J., Sircar R., Borbat P.P.,
RA Freed J.H., Watts K.J., Crane B.R.;
RT "Architecture of the soluble receptor Aer2 indicates an in-line mechanism
RT for PAS and HAMP domain signaling.";
RL J. Mol. Biol. 425:886-901(2013).
RN [14] {ECO:0007744|PDB:4I3M, ECO:0007744|PDB:4I44}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-172 OF MUTANTS GLY-33 AND
RP HIS-44 IN CHIMERIC TRANSMEMBRANE RECEPTORS.
RX PubMed=23424282; DOI=10.1371/journal.pbio.1001479;
RA Airola M.V., Sukomon N., Samanta D., Borbat P.P., Freed J.H., Watts K.J.,
RA Crane B.R.;
RT "HAMP domain conformers that propagate opposite signals in bacterial
RT chemoreceptors.";
RL PLoS Biol. 11:e1001479-e1001479(2013).
CC -!- FUNCTION: Chemoreceptor that plays a critical role in the virulence and
CC pathogenesis of P.aeruginosa in a variety of hosts (PubMed:31511598).
CC Probably acts through oxygen sensing (PubMed:31511598, PubMed:28167524,
CC PubMed:34383467). Uses a heme-based sensor (PubMed:21255112,
CC PubMed:22622145). Could be involved in chemotaxis (PubMed:12142407,
CC PubMed:14987771). When expressed in E.coli, is able to sense and
CC mediate repellent responses to oxygen, carbon monoxide and nitric oxide
CC (PubMed:21255112). {ECO:0000269|PubMed:12142407,
CC ECO:0000269|PubMed:14987771, ECO:0000269|PubMed:21255112,
CC ECO:0000269|PubMed:22622145, ECO:0000269|PubMed:28167524,
CC ECO:0000269|PubMed:31511598, ECO:0000269|PubMed:34383467}.
CC -!- SUBUNIT: Homodimer (PubMed:21255112, PubMed:23274111, PubMed:34383467).
CC The PAS domains form dimers in the presence and absence of oxygen
CC (PubMed:34383467). Interacts with the methyltransferase CheR2 via the
CC C-terminal McpB pentapeptide GWEEF (PubMed:24714571). Interacts with
CC the methylesterase/gutaminase CheB2, which also binds to the GWEEF
CC pentapeptide (PubMed:33187094). {ECO:0000269|PubMed:23274111,
CC ECO:0000269|PubMed:24714571, ECO:0000269|PubMed:33187094,
CC ECO:0000269|PubMed:34383467, ECO:0000305|PubMed:21255112}.
CC -!- INTERACTION:
CC Q9I6V6; Q9I6V6: aer2; NbExp=5; IntAct=EBI-15848257, EBI-15848257;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14987771}.
CC -!- INDUCTION: Expression is regulated by the sigma factor RpoS.
CC {ECO:0000269|PubMed:15687221}.
CC -!- DOMAIN: Contains five HAMP domains, three at the N-terminus and two at
CC the C-terminus, separated by a PAS-sensing domain (PubMed:20399181).
CC The PAS domain binds penta-coordinated b-type heme and is likely
CC responsible for sensing the gases (PubMed:21255112, PubMed:28167524).
CC Binding of oxygen induces conformational changes in the PAS-heme domain
CC (PubMed:34383467). The N-terminal HAMP domains facilitate the O(2)-
CC dependent shift of PAS to the signal-on conformation (PubMed:34383467).
CC Signals propagate from the PAS domain to the C-terminal HAMP domains
CC via a conserved DxT motif (PubMed:34383467). PAS and HAMP domains do
CC not directly interact but are arranged in a linear fashion
CC (PubMed:23274111). {ECO:0000269|PubMed:20399181,
CC ECO:0000269|PubMed:21255112, ECO:0000269|PubMed:23274111,
CC ECO:0000269|PubMed:28167524, ECO:0000269|PubMed:34383467}.
CC -!- PTM: Methylated by CheR2, but not by CheR1, CheR3 or WspC
CC (PubMed:24714571). Demethylated by CheB2 (Probable). In vitro, can be
CC methylated by E.coli CheR (PubMed:21255112).
CC {ECO:0000269|PubMed:21255112, ECO:0000269|PubMed:24714571,
CC ECO:0000305|PubMed:33187094}.
CC -!- DISRUPTION PHENOTYPE: The deletion of the gene results in an
CC attenuation of bacterial virulence in different infection models in
CC species as diverse as C.elegans, E.foetida or the insects A.bipunctata
CC and C.carnae (PubMed:31511598). Mutants have general chemotaxis defects
CC (PubMed:12142407). Mutant shows decreased aerotaxis (PubMed:14987771).
CC Aerotaxis is abolished in the aer-mcpB double mutant (PubMed:14987771).
CC {ECO:0000269|PubMed:12142407, ECO:0000269|PubMed:14987771,
CC ECO:0000269|PubMed:31511598}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; AE004091; AAG03566.1; -; Genomic_DNA.
DR PIR; A83624; A83624.
DR RefSeq; NP_248866.1; NC_002516.2.
DR RefSeq; WP_003112650.1; NZ_QZGE01000015.1.
DR PDB; 3LNR; X-ray; 2.64 A; A=1-172.
DR PDB; 3VOL; X-ray; 2.40 A; A=173-384.
DR PDB; 4HI4; X-ray; 2.30 A; A/B/D/G=174-289.
DR PDB; 4I3M; X-ray; 1.95 A; A=1-172.
DR PDB; 4I44; X-ray; 2.88 A; A=1-172.
DR PDBsum; 3LNR; -.
DR PDBsum; 3VOL; -.
DR PDBsum; 4HI4; -.
DR PDBsum; 4I3M; -.
DR PDBsum; 4I44; -.
DR AlphaFoldDB; Q9I6V6; -.
DR SMR; Q9I6V6; -.
DR STRING; 287.DR97_3132; -.
DR PaxDb; Q9I6V6; -.
DR PRIDE; Q9I6V6; -.
DR EnsemblBacteria; AAG03566; AAG03566; PA0176.
DR GeneID; 882219; -.
DR KEGG; pae:PA0176; -.
DR PATRIC; fig|208964.12.peg.182; -.
DR PseudoCAP; PA0176; -.
DR HOGENOM; CLU_000445_107_1_6; -.
DR InParanoid; Q9I6V6; -.
DR OMA; MGRCIDE; -.
DR PhylomeDB; Q9I6V6; -.
DR BioCyc; PAER208964:G1FZ6-177-MON; -.
DR EvolutionaryTrace; Q9I6V6; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0009454; P:aerotaxis; IMP:PseudoCAP.
DR GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
DR GO; GO:0052131; P:positive aerotaxis; IMP:CACAO.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR041395; HAMP_N3.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR Pfam; PF18947; HAMP_2; 1.
DR Pfam; PF18575; HAMP_N3; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF13188; PAS_8; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Metal-binding; Methylation;
KW Reference proteome; Repeat; Transducer.
FT CHAIN 1..679
FT /note="Methyl-accepting chemotaxis protein McpB"
FT /id="PRO_0000454748"
FT DOMAIN 171..213
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 333..385
FT /note="HAMP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 390..619
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 8..56
FT /note="Divergent domain HAMP 1"
FT /evidence="ECO:0000305|PubMed:20399181"
FT REGION 63..112
FT /note="Divergent domain HAMP 2"
FT /evidence="ECO:0000305|PubMed:20399181"
FT REGION 111..156
FT /note="Divergent domain HAMP 3"
FT /evidence="ECO:0000305|PubMed:20399181"
FT REGION 289..332
FT /note="Divergent domain HAMP 4"
FT /evidence="ECO:0000305|PubMed:21255112"
FT REGION 405..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 285..287
FT /note="DxT. Important for signal propagation"
FT /evidence="ECO:0000269|PubMed:34383467"
FT MOTIF 675..679
FT /note="GWEEF pentapeptide. Important for methylation by
FT CheR2"
FT /evidence="ECO:0000269|PubMed:24714571"
FT BINDING 234
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:22622145,
FT ECO:0000269|PubMed:23274111, ECO:0007744|PDB:3VOL,
FT ECO:0007744|PDB:4HI4"
FT SITE 264
FT /note="Important for gas binding and signaling"
FT /evidence="ECO:0000269|PubMed:28167524"
FT SITE 283
FT /note="Plays a crucial role in stabilization of the heme-
FT bound O(2)"
FT /evidence="ECO:0000269|PubMed:22622145,
FT ECO:0000269|PubMed:28167524"
FT MUTAGEN 1..56
FT /note="Missing: Unresponsive to O(2)."
FT /evidence="ECO:0000269|PubMed:21255112"
FT MUTAGEN 1..37
FT /note="Missing: Behaves like wild-type in a temporal O(2)
FT assay, except that it generates a slightly lower tumbling
FT bias at higher O(2) concentration."
FT /evidence="ECO:0000269|PubMed:21255112"
FT MUTAGEN 178
FT /note="A->V: Mediates wild-type responses to both O(2) and
FT CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 179
FT /note="L->C: Signal-off mutant that does not respond to
FT either O(2) or CO."
FT /evidence="ECO:0000269|PubMed:34383467"
FT MUTAGEN 187
FT /note="M->A: Signal-off mutant that does not respond to
FT either O(2) or CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 190
FT /note="D->A: Signal-off mutant that does not respond to
FT either O(2) or CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 195
FT /note="I->A,C: Signal-off mutant that does not respond to
FT either O(2) or CO."
FT /evidence="ECO:0000269|PubMed:28167524,
FT ECO:0000269|PubMed:34383467"
FT MUTAGEN 197
FT /note="Y->A: Signal-off mutant that does not respond to
FT either O(2) or CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 199
FT /note="N->A: Signal-off mutant that does not respond to
FT either O(2) or CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 202
FT /note="V->C: Signal-off mutant that does not respond to
FT either O(2) or CO."
FT /evidence="ECO:0000269|PubMed:34383467"
FT MUTAGEN 213
FT /note="I->C: Signal-off mutant that does not respond to
FT either O(2) or CO."
FT /evidence="ECO:0000269|PubMed:34383467"
FT MUTAGEN 220
FT /note="F->A: Signal-off mutant that does not respond to
FT either O(2) or CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 231
FT /note="D->A: Mediates wild-type responses to both O(2) and
FT CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 233
FT /note="F->A: Signal-off mutant that does not respond to
FT either O(2) or CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 234
FT /note="H->A: Retains 20% of heme content. Retains 6% of
FT heme content; when associated with A-239."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 237
FT /note="P->A: Mediates wild-type responses to both O(2) and
FT CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 239
FT /note="H->A: Mediates wild-type responses to both O(2) and
FT CO. Retains wild-type heme content. Retains 6% of heme
FT content; when associated with A-234."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 240
FT /note="Q->A: Mediates wild-type responses to both O(2) and
FT CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 251
FT /note="H->A: Accelerates autoxidation."
FT /evidence="ECO:0000269|PubMed:22622145"
FT MUTAGEN 264
FT /note="L->A: Locked signal-on, causing cells to tumble
FT constantly in air and in N(2)."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 264
FT /note="L->D,G,N,P,R,S,W: Signal-off receptor that does not
FT respond to the addition or removal of O(2)."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 264
FT /note="L->F: Shows a reduced tumble response to O(2).
FT Responds to CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 264
FT /note="L->I,Q: Shows wild-type O(2) responses."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 264
FT /note="L->K: Signal-off mutant that does not respond to the
FT addition or removal of O(2). Does not bind either O(2) or
FT CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 264
FT /note="L->V: Mediates an O(2) response but exhibits a 30-
FT sec-delayed smooth-swimming response in N(2) and does not
FT respond to CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 278
FT /note="G->A: Signal-off mutant that does not respond to
FT either O(2) or CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 283
FT /note="W->A,C,G,H,K,P,Q,R,S,T,Y: Signal-off mutant that
FT does not respond to the addition or removal of O(2)."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 283
FT /note="W->F: Signal-on-biased mutant. 50 to 80% of the
FT cells continue to tumble when air is removed. Can still
FT bind O(2) in vitro."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 283
FT /note="W->I: Inverted phenotype. Cannot form stable O(2)
FT bound in vitro. Responds to CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 283
FT /note="W->L: Cannot form stable O(2) bound in vitro.
FT Signal-on-biased mutant. 50 to 80% of the cells continue to
FT tumble when air is removed."
FT /evidence="ECO:0000269|PubMed:22622145,
FT ECO:0000269|PubMed:28167524"
FT MUTAGEN 283
FT /note="W->V: Does not respond to the addition or removal of
FT O(2). Responds to CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 285
FT /note="D->A: Signal-off mutant that does not respond to
FT either O(2) or CO."
FT /evidence="ECO:0000269|PubMed:28167524"
FT MUTAGEN 289..379
FT /note="Missing: Kinase-on mutant that is unresponsive to
FT changes in O(2) concentrations."
FT /evidence="ECO:0000269|PubMed:21255112"
FT MUTAGEN 675..679
FT /note="Missing: Abolishes interaction with CheR2 and
FT methylation."
FT /evidence="ECO:0000269|PubMed:24714571"
FT HELIX 8..26
FT /evidence="ECO:0007829|PDB:4I3M"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:4I3M"
FT HELIX 42..80
FT /evidence="ECO:0007829|PDB:4I3M"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:4I3M"
FT HELIX 95..126
FT /evidence="ECO:0007829|PDB:4I3M"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4I3M"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:4I3M"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:4HI4"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:4HI4"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:4HI4"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:4HI4"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:4HI4"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:4HI4"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:4HI4"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:3VOL"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:4HI4"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:4HI4"
FT STRAND 260..270
FT /evidence="ECO:0007829|PDB:4HI4"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:4HI4"
FT HELIX 287..304
FT /evidence="ECO:0007829|PDB:3VOL"
SQ SEQUENCE 679 AA; 72591 MW; 246EF0D775120272 CRC64;
MGLFNAHAVA QQRADRIATL LQSFADGQLD TAVGEAPAPG YERLYDSLRA LQRQLREQRA
ELQQVESLEA GLAEMSRQHE AGWIDQTIPA ERLEGRAARI AKGVNELVAA HIAVKMKVVS
VVTAYGQGNF EPLMDRLPGK KAQITEAIDG VRERLRGAAE ATSAQLATAA YNARIKSALD
NVSANVMIAD NDLNIIYMNR TVSEMLGRAE ADIRKQLPNF DAGRLMGANI DVFHKNPAHQ
RHLLANLTGV HKAELNLGGR RFSLDVVPVF NDANERLGSA VQWTDRTEEH RAEQEVSQLV
QAAAAGDFSK RVEEAGKEGF FLRLAKDLNS LVDTADRGLR DVSRMLGALA QGDLTQRIEA
DYQGTFGQLK DFSNDTAQSL SRMLGQIREA ADTINTAASE IASGNAELSA RTEQQASSLE
ETASSMEELT STVKLNAENA RQANSLAANA SEVATQGGTV VQKVVSTMSS INESARKIAD
IIGVIDGIAF QTNILALNAA VEAARAGEQG RGFAVVAGEV RTLAQRSAAA AKEIKTLISD
SVDKVENGNT LVAQAGQTMS DIVVAIRRVT DIMSEIAAAS AEQSTGIEEV NSAVSQMDDM
TQQNAALVEE AAAAAEAMQE QAGLLNQSVA VFRLDTPPSV VQLASARPSA PRPSAPAPLA
RSGMARASKA RKEDGWEEF
