PCAY_PSEPK
ID PCAY_PSEPK Reviewed; 550 AA.
AC Q88JK6;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Methyl-accepting chemotaxis protein PcaY {ECO:0000305};
DE AltName: Full=PcaY_PP {ECO:0000303|PubMed:28620365};
GN Name=pcaY {ECO:0000303|PubMed:12534463};
GN OrderedLocusNames=PP_2643 {ECO:0000312|EMBL:AAN68251.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=28620365; DOI=10.3389/fmicb.2017.00990;
RA Fernandez M., Matilla M.A., Ortega A., Krell T.;
RT "Metabolic value chemoattractants are preferentially recognized at broad
RT ligand range chemoreceptor of Pseudomonas putida KT2440.";
RL Front. Microbiol. 8:990-990(2017).
RN [3] {ECO:0007744|PDB:6S18, ECO:0007744|PDB:6S1A, ECO:0007744|PDB:6S33, ECO:0007744|PDB:6S37, ECO:0007744|PDB:6S38, ECO:0007744|PDB:6S3B}
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 47-190 OF APOPROTEIN AND IN
RP COMPLEXES WITH PROTOCATECHUATE; QUINATE; BENZOATE AND 2-HYDROXYBENZOIC
RP ACID, DOMAIN, AND MUTAGENESIS OF ARG-71; SER-73; ASN-75; SER-78; GLN-142
RP AND ASN-158.
RX PubMed=33021055; DOI=10.1111/febs.15580;
RA Gavira J.A., Matilla M.A., Fernandez M., Krell T.;
RT "The structural basis for signal promiscuity in a bacterial
RT chemoreceptor.";
RL FEBS J. 288:2294-2310(2021).
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 (Probable). PcaY recognizes a wide range of compounds
CC containing a C6-membered ring with a carboxylate group. Binds
CC preferentially compounds that serve as carbon sources and among them
CC those that rapidly promote growth. Tightest binding compounds are
CC quinate, shikimate, 3-dehydroshikimate and protocatechuate, which are
CC at the interception of the biosynthetic shikimate and catabolic quinate
CC pathways (PubMed:28620365). {ECO:0000269|PubMed:28620365, ECO:0000305}.
CC -!- SUBUNIT: Ligand free PcaY_PP-ligand-binding domain (LBD) is present in
CC a monomer-dimer equilibrium (PubMed:28620365). Only the dimeric LBD is
CC able to bind ligands which in turn causes dimer stabilization
CC (PubMed:28620365). {ECO:0000269|PubMed:28620365}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DOMAIN: The ligand-binding domain (LBD) forms a four-helix bundle
CC (4HB), and both ligand binding sites of the dimer are occupied with the
CC high-affinity ligands protocatechuate and quinate, whereas the lower-
CC affinity ligands benzoate and salicylate are present in only one site.
CC Ligand binding causes rigid-body scissoring movements of both monomers
CC of the dimer. {ECO:0000269|PubMed:33021055}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene abolishes chemotaxis to
CC benzoate, quinate, protocatechuate and shikimate. Inactivation of the
CC gene does not alter competitive plant root colonization.
CC {ECO:0000269|PubMed:28620365}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; AE015451; AAN68251.1; -; Genomic_DNA.
DR RefSeq; NP_744787.1; NC_002947.4.
DR PDB; 6S18; X-ray; 1.60 A; A/B=1-550.
DR PDB; 6S1A; X-ray; 2.11 A; A/B=1-550.
DR PDB; 6S33; X-ray; 1.56 A; A/B=1-550.
DR PDB; 6S37; X-ray; 2.30 A; A/B=1-550.
DR PDB; 6S38; X-ray; 2.15 A; A/B=1-550.
DR PDB; 6S3B; X-ray; 1.95 A; A/B=1-550.
DR PDBsum; 6S18; -.
DR PDBsum; 6S1A; -.
DR PDBsum; 6S33; -.
DR PDBsum; 6S37; -.
DR PDBsum; 6S38; -.
DR PDBsum; 6S3B; -.
DR SMR; Q88JK6; -.
DR STRING; 160488.PP_2643; -.
DR EnsemblBacteria; AAN68251; AAN68251; PP_2643.
DR KEGG; ppu:PP_2643; -.
DR PATRIC; fig|160488.4.peg.2804; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_27_6; -.
DR OMA; IEQMIGS; -.
DR PhylomeDB; Q88JK6; -.
DR BioCyc; PPUT160488:G1G01-2824-MON; -.
DR Proteomes; UP000000556; 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:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR003122; Tar_rcpt_lig-bd.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF02203; TarH; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 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..550
FT /note="Methyl-accepting chemotaxis protein PcaY"
FT /id="PRO_0000454714"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..198
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..550
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 221..273
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 278..514
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 44..196
FT /note="Ligand-binding domain"
FT /evidence="ECO:0000305|PubMed:28620365"
FT BINDING 71..78
FT /ligand="3,4-dihydroxybenzoate"
FT /ligand_id="ChEBI:CHEBI:36241"
FT /evidence="ECO:0000269|PubMed:33021055,
FT ECO:0007744|PDB:6S33"
FT BINDING 71..78
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000269|PubMed:33021055,
FT ECO:0000312|PDB:6S38"
FT BINDING 71
FT /ligand="benzoate"
FT /ligand_id="ChEBI:CHEBI:16150"
FT /evidence="ECO:0000269|PubMed:33021055,
FT ECO:0007744|PDB:6S3B"
FT BINDING 71
FT /ligand="salicylate"
FT /ligand_id="ChEBI:CHEBI:30762"
FT /evidence="ECO:0000269|PubMed:33021055,
FT ECO:0007744|PDB:6S37"
FT BINDING 75
FT /ligand="benzoate"
FT /ligand_id="ChEBI:CHEBI:16150"
FT /evidence="ECO:0000269|PubMed:33021055,
FT ECO:0007744|PDB:6S3B"
FT BINDING 75
FT /ligand="salicylate"
FT /ligand_id="ChEBI:CHEBI:30762"
FT /evidence="ECO:0000269|PubMed:33021055,
FT ECO:0007744|PDB:6S37"
FT BINDING 135
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000269|PubMed:33021055,
FT ECO:0000312|PDB:6S38"
FT BINDING 135
FT /ligand="salicylate"
FT /ligand_id="ChEBI:CHEBI:30762"
FT /evidence="ECO:0000269|PubMed:33021055,
FT ECO:0007744|PDB:6S37"
FT BINDING 142
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000269|PubMed:33021055,
FT ECO:0000312|PDB:6S38"
FT BINDING 158
FT /ligand="L-quinate"
FT /ligand_id="ChEBI:CHEBI:29751"
FT /evidence="ECO:0000269|PubMed:33021055,
FT ECO:0000312|PDB:6S38"
FT BINDING 169
FT /ligand="3,4-dihydroxybenzoate"
FT /ligand_id="ChEBI:CHEBI:36241"
FT /evidence="ECO:0000269|PubMed:33021055,
FT ECO:0007744|PDB:6S33"
FT MUTAGEN 71
FT /note="R->A: Abolishes binding of all ligands."
FT /evidence="ECO:0000269|PubMed:33021055"
FT MUTAGEN 73
FT /note="S->A: Abolishes binding of quinate and
FT protocatechuate, and shows reduced affinity for benzoate
FT and salicylate."
FT /evidence="ECO:0000269|PubMed:33021055"
FT MUTAGEN 75
FT /note="N->A: Abolishes binding of benzoate and
FT protocatechuate, and shows reduced affinity for quinate and
FT salicylate."
FT /evidence="ECO:0000269|PubMed:33021055"
FT MUTAGEN 78
FT /note="S->A: Does not significantly alter binding of
FT benzoate and protocatechuate."
FT /evidence="ECO:0000269|PubMed:33021055"
FT MUTAGEN 142
FT /note="Q->A: Strong decrease in quinate binding and small
FT decrease in affinity for salicylate."
FT /evidence="ECO:0000269|PubMed:33021055"
FT MUTAGEN 158
FT /note="N->A: Strong decrease in quinate binding and small
FT decrease in affinity for salicylate."
FT /evidence="ECO:0000269|PubMed:33021055"
FT HELIX 48..84
FT /evidence="ECO:0007829|PDB:6S33"
FT HELIX 88..115
FT /evidence="ECO:0007829|PDB:6S33"
FT HELIX 119..147
FT /evidence="ECO:0007829|PDB:6S33"
FT HELIX 151..187
FT /evidence="ECO:0007829|PDB:6S33"
SQ SEQUENCE 550 AA; 59486 MW; 2FDCB0C0A7C5431F CRC64;
MVPTRSTARM LANLKIRTGM FWVLSLFSLT LLFSTASAWW AALGSDQQIT ELDQTAHQSD
RLNNALLMAI RSSANVSSGF IEQLGGHDES AGKRMALSVE LNNKSQALVD EFVENAREPA
LRGLATELQA TFAEYAKAVA GQREATRQRS LEQYFKVNSD AGNAMGRLQT LRQQLVTTLS
ERGQQIMLES DRRLARAQLL SLCLLGVTVV LAVLCWAFIA QRVLHPLREA GGHFRRIASG
DLSVPVQGQG NNEIGQLFHE LQRMQQSQRD TLGQINNCAR QLDAAATALN AVTEESANNL
RQQGQELEQA ATAVTEMTTA VEEVARNAIT TSQTTSESNQ LAAQSRRQVS ENIDGTEAMT
REIQTSSAHL QQLVGQVRDI GKVLEVIRSV SEQTNLLALN AAIEAARAGE AGRGFAVVAD
EVRTLAYRTQ QSTQEIEQMI GSVQAGTEAA VASMQASTNR AQSTLDVTLA SGQVLEGIYS
AIGEINERNL VIASAAEEQA QVAREVDRNL LNIRELSNHS AAGAQQTSEA SKALSGLVGE
MTALVGRFKV
