PCTA_PSEAE
ID PCTA_PSEAE Reviewed; 629 AA.
AC G3XD24; O32442; Q51509; Q7DC77;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Methyl-accepting chemotaxis protein PctA;
GN Name=pctA; OrderedLocusNames=PA4309;
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=8522505; DOI=10.1128/jb.177.24.7019-7025.1995;
RA Kuroda A., Kumano T., Taguchi K., Nikata T., Kato J., Ohtake H.;
RT "Molecular cloning and characterization of a chemotactic transducer gene in
RT Pseudomonas aeruginosa.";
RL J. Bacteriol. 177:7019-7025(1995).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ARG-126; TRP-128; TYR-144;
RP ASP-146 AND ASP-173.
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 [6]
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=30425146; DOI=10.1128/mbio.01894-18;
RA Corral-Lugo A., Matilla M.A., Martin-Mora D., Silva Jimenez H.,
RA Mesa Torres N., Kato J., Hida A., Oku S., Conejero-Muriel M., Gavira J.A.,
RA Krell T.;
RT "High-affinity chemotaxis to histamine mediated by the TlpQ chemoreceptor
RT of the human pathogen Pseudomonas aeruginosa.";
RL MBio 9:e01894-e01894(2018).
RN [8]
RP FUNCTION IN RESPONSE TO AI-2, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP TYR-101; MET-111; TYR-121; ARG-126; TRP-128; TYR-144; ASP-146; ALA-147 AND
RP ASP-173.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=33097715; DOI=10.1038/s41467-020-19243-5;
RA Zhang L., Li S., Liu X., Wang Z., Jiang M., Wang R., Xie L., Liu Q.,
RA Xie X., Shang D., Li M., Wei Z., Wang Y., Fan C., Luo Z.Q., Shen X.;
RT "Sensing of autoinducer-2 by functionally distinct receptors in
RT prokaryotes.";
RL Nat. Commun. 11:5371-5371(2020).
RN [9] {ECO:0007744|PDB:5LTX, ECO:0007744|PDB:5T65, ECO:0007744|PDB:5T7M}
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 30-278 IN COMPLEXES WITH
RP METHIONINE; ISOLEUCINE AND TRYPTOPHAN, 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. Major receptor that responds to all naturally occurring L-
CC amino acids, except L-Gln and L-Asp. Also involved in repellent
CC responses to trichloroethylene (TCE), chloroform and methylthiocyanate
CC (PubMed:16233808, PubMed:23650915, PubMed:8522505, PubMed:9353923).
CC Also mediates chemotaxis to histamine, but does not bind histamine
CC (PubMed:30425146). In addition, binds the quorum-sensing signal
CC autoinducer 2 (AI-2), thus inducing chemotaxis toward AI-2 and biofilm
CC formation (PubMed:33097715). {ECO:0000269|PubMed:16233808,
CC ECO:0000269|PubMed:23650915, ECO:0000269|PubMed:30425146,
CC ECO:0000269|PubMed:33097715, ECO:0000269|PubMed:8522505,
CC 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 17 L-amino acids.
CC {ECO:0000269|PubMed:23650915}.
CC -!- DISRUPTION PHENOTYPE: Mutant is defective in taxis toward 17 amino
CC acids, including Gly, L-Ser, L-Thr and L-Val. Mutant shows also
CC decreased chemotactic responses to TCE, chloroform and
CC methylthiocyanate (PubMed:16233808, PubMed:8522505, PubMed:9353923).
CC Deletion of pctA, pctB and pctC abolishes chemotaxis to 5 mM histamine,
CC but significant chemotaxis is observed at a concentration range between
CC 500 nM and 500 uM (PubMed:30425146). The pctABC-tlpQ deletion mutant is
CC devoid of histamine chemotaxis over the entire concentration range (50
CC nM to 50 mM) (PubMed:30425146). Deletion of the gene significantly
CC reduces chemotaxis to AI-2 (PubMed:33097715). The deletion mutant does
CC not show significant reduction in swarming or immobilization near
CC epithelial wounds, but the pctABC triple deletion mutant shows a
CC significant reduction in chemotaxis and immobilization along wounds of
CC human cystic fibrosis airway epithelial cells (PubMed:27031335).
CC {ECO:0000269|PubMed:16233808, ECO:0000269|PubMed:27031335,
CC ECO:0000269|PubMed:30425146, ECO:0000269|PubMed:33097715,
CC ECO:0000269|PubMed:8522505, 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; D50642; BAA09307.1; -; Genomic_DNA.
DR EMBL; D86947; BAA23412.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07697.1; -; Genomic_DNA.
DR PIR; B83107; B83107.
DR RefSeq; NP_252999.1; NC_002516.2.
DR RefSeq; WP_003148125.1; NZ_CP053028.1.
DR PDB; 5LTX; X-ray; 2.02 A; A/B=30-278.
DR PDB; 5T65; X-ray; 2.20 A; A/B=30-278.
DR PDB; 5T7M; X-ray; 2.25 A; A/B=30-278.
DR PDBsum; 5LTX; -.
DR PDBsum; 5T65; -.
DR PDBsum; 5T7M; -.
DR AlphaFoldDB; G3XD24; -.
DR SMR; G3XD24; -.
DR STRING; 287.DR97_1484; -.
DR PaxDb; G3XD24; -.
DR EnsemblBacteria; AAG07697; AAG07697; PA4309.
DR GeneID; 881565; -.
DR KEGG; pae:PA4309; -.
DR PATRIC; fig|208964.12.peg.4513; -.
DR PseudoCAP; PA4309; -.
DR HOGENOM; CLU_000445_107_19_6; -.
DR InParanoid; G3XD24; -.
DR OMA; RDQTYMM; -.
DR PhylomeDB; G3XD24; -.
DR BioCyc; PAER208964:G1FZ6-4393-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:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR000727; T_SNARE_dom.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
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 PctA"
FT /id="PRO_0000424849"
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 36..259
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 121
FT /ligand="L-isoleucine"
FT /ligand_id="ChEBI:CHEBI:58045"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5T65"
FT BINDING 121
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LTX"
FT BINDING 121
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5T7M"
FT BINDING 126..128
FT /ligand="L-isoleucine"
FT /ligand_id="ChEBI:CHEBI:58045"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5T65"
FT BINDING 126..128
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LTX"
FT BINDING 126..128
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5T7M"
FT BINDING 144..147
FT /ligand="L-isoleucine"
FT /ligand_id="ChEBI:CHEBI:58045"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5T65"
FT BINDING 144..147
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LTX"
FT BINDING 144..147
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5T7M"
FT BINDING 173
FT /ligand="L-isoleucine"
FT /ligand_id="ChEBI:CHEBI:58045"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5T65"
FT BINDING 173
FT /ligand="L-methionine"
FT /ligand_id="ChEBI:CHEBI:57844"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5LTX"
FT BINDING 173
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000269|PubMed:31964737,
FT ECO:0000312|PDB:5T7M"
FT MUTAGEN 101
FT /note="Y->A: 260-fold reduction in AI-2 binding affinity."
FT /evidence="ECO:0000269|PubMed:33097715"
FT MUTAGEN 111
FT /note="M->A: 120-fold reduction in AI-2 binding affinity."
FT /evidence="ECO:0000269|PubMed:33097715"
FT MUTAGEN 121
FT /note="Y->A: 150-fold reduction in AI-2 binding affinity."
FT /evidence="ECO:0000269|PubMed:33097715"
FT MUTAGEN 126
FT /note="R->A: Fails to recognize L-Ala, L-Arg, L-Thr, L-Trp
FT and L-Pro. 290-fold reduction in AI-2 binding affinity."
FT /evidence="ECO:0000269|PubMed:23650915,
FT ECO:0000269|PubMed:33097715"
FT MUTAGEN 128
FT /note="W->A: Fails to recognize L-Trp. Decreases affinity
FT for L-Ala, L-Arg, L-Thr and L-Pro. 160-fold reduction in
FT AI-2 binding affinity."
FT /evidence="ECO:0000269|PubMed:23650915,
FT ECO:0000269|PubMed:33097715"
FT MUTAGEN 144
FT /note="Y->A: Binds L-Trp, but not L-Ala, L-Arg, L-Thr and
FT L-Pro. 100-fold reduction in AI-2 binding affinity."
FT /evidence="ECO:0000269|PubMed:23650915,
FT ECO:0000269|PubMed:33097715"
FT MUTAGEN 146
FT /note="D->A: Fails to recognize L-Ala, L-Arg, L-Thr, L-Trp
FT and L-Pro. 240-fold reduction in AI-2 binding affinity."
FT /evidence="ECO:0000269|PubMed:23650915,
FT ECO:0000269|PubMed:33097715"
FT MUTAGEN 147
FT /note="A->F: 80-fold reduction in AI-2 binding affinity."
FT /evidence="ECO:0000269|PubMed:33097715"
FT MUTAGEN 173
FT /note="D->A: Binds L-Trp, but not L-Ala, L-Arg, L-Thr and
FT L-Pro. 85-fold reduction in AI-2 binding affinity."
FT /evidence="ECO:0000269|PubMed:23650915,
FT ECO:0000269|PubMed:33097715"
FT CONFLICT 570..571
FT /note="SV -> VL (in Ref. 2; BAA23412)"
FT /evidence="ECO:0000305"
FT HELIX 31..77
FT /evidence="ECO:0007829|PDB:5LTX"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:5LTX"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:5LTX"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:5LTX"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:5LTX"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5LTX"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:5LTX"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:5LTX"
FT STRAND 151..162
FT /evidence="ECO:0007829|PDB:5LTX"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:5LTX"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:5LTX"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:5LTX"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:5LTX"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:5LTX"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:5LTX"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:5LTX"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:5LTX"
FT STRAND 227..236
FT /evidence="ECO:0007829|PDB:5LTX"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:5LTX"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:5LTX"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:5LTX"
SQ SEQUENCE 629 AA; 68017 MW; 714BA6C4DAC6725C CRC64;
MIKSLKFSHK ILLAASLVVF AAFALFTLYN DYLQRNAIRE DLESYLREMG DVTSSNIQNW
LGGRLLLVEQ TAQTLARDHS PETVSALLEQ PALTSTFSFT YLGQQDGVFT MRPDSPMPAG
YDPRSRPWYK DAVAAGGLTL TEPYVDAATQ ELIITAATPV KAAGNTLGVV GGDLSLKTLV
QIINSLDFSG MGYAFLVSGD GKILVHPDKE QVMKTLSEVY PQNTPKIATG FSEAELHGHT
RILAFTPIKG LPSVTWYLAL SIDKDKAYAM LSKFRVSAIA AALISIVAIL VLLGLLIRLL
MQPLHLMGRA MQDIAQGEGD LTKRLAVTSR DEFGVLGDAF NQFVERIHRS IREVAGTAHK
LHDVSQLVVN ASNSSMANSD EQSNRTNSVA AAINELGAAA QEIARNAADA SHHASDANHQ
AEDGKQVVEQ TIRAMNELSE KISASCANIE ALNSRTVNIG QILEVIKGIS EQTNLLALNA
AIEAARAGEA GRGFAVVADE VRNLAHRAQE SAQQIQKMIE ELQVGAREAV ATMTESQRYS
LESVEIANRA GESLSSVTRR IGEIDGMNQS VATATEEQTA VVDSLNMDIT EINTLNQEGV
ENLQATLRAC GELETQAGRL RQLVDSFKI
