PCAY_PSEP1
ID PCAY_PSEP1 Reviewed; 541 AA.
AC A5W2C8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Methyl-accepting chemotaxis protein PcaY {ECO:0000305};
DE AltName: Full=Aromatic acid chemoreceptor PcaY {ECO:0000303|PubMed:25582673};
GN Name=pcaY {ECO:0000303|PubMed:25582673};
GN OrderedLocusNames=Pput_2149 {ECO:0000312|EMBL:ABQ78288.1};
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RX PubMed=25582673; DOI=10.1111/mmi.12929;
RA Luu R.A., Kootstra J.D., Nesteryuk V., Brunton C.N., Parales J.V.,
RA Ditty J.L., Parales R.E.;
RT "Integration of chemotaxis, transport and catabolism in Pseudomonas putida
RT and identification of the aromatic acid chemoreceptor PcaY.";
RL Mol. Microbiol. 96:134-147(2015).
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 is responsible for the detection of
CC multiple aromatic and hydroaromatic compounds that are metabolized
CC through the beta-ketoadipate catabolic pathway, including vanillin,
CC vanillate, 4-hydroxybenzoate (4-HBA), benzoate and protocatechuate. It
CC also senses several nonmetabolizable aromatic compounds
CC (PubMed:25582673). {ECO:0000269|PubMed:25582673, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:25582673}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expression is induced by beta-ketoadipate, via the
CC transcriptional activator PcaR. {ECO:0000269|PubMed:25582673}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant does not respond to vanillate and
CC shows reduced responses to 4-HBA, benzoate, protocatechuate and
CC vanillin. {ECO:0000269|PubMed:25582673}.
CC -!- MISCELLANEOUS: It could not be ruled out that downstream intermediates
CC are sensed by the chemoreceptor rather than the hydroaromatic compounds
CC themselves. {ECO:0000305|PubMed:25582673}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; CP000712; ABQ78288.1; -; Genomic_DNA.
DR RefSeq; WP_012052060.1; NC_009512.1.
DR SMR; A5W2C8; -.
DR STRING; 351746.Pput_2149; -.
DR EnsemblBacteria; ABQ78288; ABQ78288; Pput_2149.
DR KEGG; ppf:Pput_2149; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_27_6; -.
DR OMA; IEQMIGS; -.
DR OrthoDB; 429006at2; -.
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 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Chemotaxis; Membrane; Methylation;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..541
FT /note="Methyl-accepting chemotaxis protein PcaY"
FT /id="PRO_0000454713"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25582673"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..189
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:25582673"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:25582673"
FT DOMAIN 212..264
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 269..505
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 35..187
FT /note="Ligand-binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q88JK6"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 58562 MW; CEFF1C118F45B3E2 CRC64;
MLANLKIRTG MFWVLSLFSL TLLFSTASAW WAAVGSDQQI TELDQTAHQS DRLNNALLMA
IRSSANVSSG FIEQLGGHDE SAGKRMALSV ELNNKSQTLV DEFVENAREP ALRVLATELQ
ATFAEYAKAV AGQREATRQR SLEQYFKVNS DAGNAMGRLQ TLRQQLVTTL SERGQQIMLE
SDRRLARAQL LSLCLLGMTV VLAVLCWAFI AQRVLHPLRE AGGHFRRIAS GDLSVPVQGQ
GNNEIGQLFH ELQRMQQSQR DTLGQINNCA RQLDAAASAL NAVTEESANN LRQQGQELEQ
AATAVTEMTT AVEEVARNAI TTSQTTSESN QLAAQSRRQV SENIDGTEAM TREIQTSSAH
LQQLVGQVRD IGKVLEVIRS VSEQTNLLAL NAAIEAARAG EAGRGFAVVA DEVRTLAYRT
QQSTQEIEQM IGSVQAGTEA AVASMQASTN RAQSTLDVTL ASGQVLEGIY SAIGEINERN
LVIASAAEEQ AQVAREVDRN LLNIRELSNH SAAGAQQTSE ASKALSGLVG EMTALVGRFK
V
