PCTB_PSEAE
ID PCTB_PSEAE Reviewed; 629 AA.
AC Q9HW91; O32443;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Methyl-accepting chemotaxis protein PctB;
GN Name=pctB; OrderedLocusNames=PA4310;
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 [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9353923; DOI=10.1099/00221287-143-10-3223;
RA Taguchi K., Fukutomi H., Kuroda A., Kato J., Ohtake H.;
RT "Genetic identification of chemotactic transducers for amino acids in
RT Pseudomonas aeruginosa.";
RL Microbiology 143:3223-3229(1997).
RN [2]
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 [3]
RP FUNCTION IN REPELLENT RESPONSES, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=16233808; DOI=10.1263/jbb.99.396;
RA Shitashiro M., Tanaka H., Hong C.S., Kuroda A., Takiguchi N., Ohtake H.,
RA Kato J.;
RT "Identification of chemosensory proteins for trichloroethylene in
RT Pseudomonas aeruginosa.";
RL J. Biosci. Bioeng. 99:396-402(2005).
RN [4]
RP FUNCTION, SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=23650915; DOI=10.1111/mmi.12255;
RA Rico-Jimenez M., Munoz-Martinez F., Garcia-Fontana C., Fernandez M.,
RA Morel B., Ortega A., Ramos J.L., Krell T.;
RT "Paralogous chemoreceptors mediate chemotaxis towards protein amino acids
RT and the non-protein amino acid gamma-aminobutyrate (GABA).";
RL Mol. Microbiol. 88:1230-1243(2013).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=27031335; DOI=10.1371/journal.pone.0150109;
RA Schwarzer C., Fischer H., Machen T.E.;
RT "Chemotaxis and binding of Pseudomonas aeruginosa to scratch-wounded human
RT cystic fibrosis airway epithelial cells.";
RL PLoS ONE 11:e0150109-e0150109(2016).
RN [6] {ECO:0007744|PDB:5LT9, ECO:0007744|PDB:5LTO}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 30-277 IN COMPLEXES WITH
RP GLUTAMINE AND ARGININE, AND MOLECULAR EVOLUTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=31964737; DOI=10.1128/mbio.03066-19;
RA Gavira J.A., Gumerov V.M., Rico-Jimenez M., Petukh M., Upadhyay A.A.,
RA Ortega A., Matilla M.A., Zhulin I.B., Krell T.;
RT "How bacterial chemoreceptors evolve novel ligand specificities.";
RL MBio 11:e03066-e03066(2020).
CC -!- FUNCTION: Chemotactic-signal transducers respond to changes in the
CC concentration of attractants and repellents in the environment,
CC transduce a signal from the outside to the inside of the cell, and
CC facilitate sensory adaptation through the variation of the level of
CC methylation. Responds to L-Arg, L-Gln, L-Ala, L-Glu, L-Lys, L-Met and
CC L-Tyr. Also involved in repellent responses to trichloroethylene (TCE),
CC chloroform and methylthiocyanate. {ECO:0000269|PubMed:16233808,
CC ECO:0000269|PubMed:23650915, ECO:0000269|PubMed:9353923}.
CC -!- SUBUNIT: Monomer in the absence and presence of ligands.
CC {ECO:0000269|PubMed:23650915}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DOMAIN: The ligand binding region binds directly to 5 L-amino acids.
CC {ECO:0000269|PubMed:23650915}.
CC -!- DISRUPTION PHENOTYPE: Mutant is defective in taxis toward L-Gln. Mutant
CC shows also decreased chemotactic responses to TCE, chloroform and
CC methylthiocyanate (PubMed:16233808, PubMed:9353923). The deletion
CC mutant does not show significant reduction in swarming or
CC immobilization near epithelial wounds, but the pctABC triple deletion
CC mutant shows a significant reduction in chemotaxis and immobilization
CC along wounds of human cystic fibrosis airway epithelial cells
CC (PubMed:27031335). {ECO:0000269|PubMed:16233808,
CC ECO:0000269|PubMed:27031335, ECO:0000269|PubMed:9353923}.
CC -!- MISCELLANEOUS: PctA has a broad ligand range and responds to most of
CC the proteinogenic amino acids, whereas PctB and PctC have a much
CC narrower range and show strong ligand preference for L-glutamine and
CC gamma-aminobutyrate, respectively. These receptors are paralogs: pctA
CC gene duplication in the common ancestor of the genus Pseudomonas led to
CC pctC, whereas pctB originated through another, independent pctA
CC duplication. {ECO:0000305|PubMed:31964737}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; D86947; BAA23413.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07698.1; -; Genomic_DNA.
DR PIR; C83107; C83107.
DR RefSeq; NP_253000.1; NC_002516.2.
DR RefSeq; WP_003148126.1; NZ_QZGA01000014.1.
DR PDB; 5LT9; X-ray; 3.00 A; A/B=30-277.
DR PDB; 5LTO; X-ray; 3.46 A; A/B=30-277.
DR PDBsum; 5LT9; -.
DR PDBsum; 5LTO; -.
DR AlphaFoldDB; Q9HW91; -.
DR SMR; Q9HW91; -.
DR STRING; 287.DR97_1485; -.
DR PaxDb; Q9HW91; -.
DR PRIDE; Q9HW91; -.
DR EnsemblBacteria; AAG07698; AAG07698; PA4310.
DR GeneID; 881566; -.
DR KEGG; pae:PA4310; -.
DR PATRIC; fig|208964.12.peg.4514; -.
DR PseudoCAP; PA4310; -.
DR HOGENOM; CLU_000445_107_19_6; -.
DR InParanoid; Q9HW91; -.
DR OMA; YMYYSYA; -.
DR PhylomeDB; Q9HW91; -.
DR BioCyc; PAER208964:G1FZ6-4394-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016597; F:amino acid binding; IDA:PseudoCAP.
DR GO; GO:0006935; P:chemotaxis; IMP:PseudoCAP.
DR GO; GO:0043200; P:response to amino acid; IMP:PseudoCAP.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029151; Sensor-like_sf.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF103190; SSF103190; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Chemotaxis; Membrane;
KW Methylation; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..629
FT /note="Methyl-accepting chemotaxis protein PctB"
FT /id="PRO_0000424850"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..276
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..260
FT /note="Cache"
FT /evidence="ECO:0000255"
FT DOMAIN 298..352
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 357..593
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 405..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LT9"
FT BINDING 115
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LT9"
FT BINDING 115
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LTO"
FT BINDING 121
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LT9"
FT BINDING 121
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LTO"
FT BINDING 126..128
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LT9"
FT BINDING 126..128
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LTO"
FT BINDING 144..146
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LTO"
FT BINDING 146
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LT9"
FT BINDING 173
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LT9"
FT BINDING 173
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LTO"
FT CONFLICT 16
FT /note="A -> E (in Ref. 1; BAA23413)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="R -> L (in Ref. 1; BAA23413)"
FT /evidence="ECO:0000305"
FT HELIX 42..77
FT /evidence="ECO:0007829|PDB:5LT9"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:5LT9"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:5LT9"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:5LT9"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:5LT9"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5LT9"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:5LT9"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:5LTO"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:5LT9"
FT STRAND 151..164
FT /evidence="ECO:0007829|PDB:5LT9"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:5LT9"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:5LT9"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:5LT9"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:5LT9"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:5LT9"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:5LT9"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:5LT9"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:5LT9"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:5LT9"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:5LT9"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:5LT9"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:5LT9"
SQ SEQUENCE 629 AA; 68077 MW; CA1A12D76319CF52 CRC64;
MIKSLKFSHK ILLAAALVVI ATFSLFTLYN DSLQRASIRE DLEDYLHEMG EITASNVQNW
LSGRILLIEN LAQTLARDHS PETTQALLEQ PLLGSTFLFT YLGQTDGTYT ARPTSDLPAD
YDPRRRPWYN AATSAGQTTL TEPYMEPAIH ELVLTIASPA RQGGQPFGVV GGDLSLQTVV
KIINSLDFGG MGYAFLVSGD GKILVHPDKD QVMKSLSDVY PRNTPKIGSG FSEAELHGNT
RILSFSPVKG LSGLDWYIGI SVDKDKAYAM LTKLRTSAIV AALIAVVAIV LLLGMLIRVL
MQPLTDMGRA MQDIAQGEGD LTKRLKVTSN DEFGALAISF NRFVERIHES IREVAGTARQ
LHDVAQLVVN ASNSSMANSD EQSNRTNSVA AAINELGAAA QEIARNAADA SHHASDANHQ
AEDGKQVVEQ TIRAMNELSE KISASCANIE ALNSRTVNIG QILEVIKGIS EQTNLLALNA
AIEAARAGEA GRGFAVVADE VRNLAHRAQE SAQQIQKMIE ELQIGAQEAV STMTESQRYS
LESVEIANRA GERLSSVTGR IAEIDGMNQS VATATEEQTA VVDSLNMDIT EINTLNQEGV
ENLQATLRAC GELETQAGRL RQLVDSFKI
