TLPQ_PSEAE
ID TLPQ_PSEAE Reviewed; 714 AA.
AC Q9I0I4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Methyl-accepting chemotaxis protein TlpQ {ECO:0000305};
DE AltName: Full=TlpQ chemoreceptor {ECO:0000303|PubMed:30425146};
GN Name=tlpQ {ECO:0000303|PubMed:30425146};
GN OrderedLocusNames=PA2654 {ECO:0000312|EMBL:AAG06042.1};
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 RESPONSE TO AI-2, AND DISRUPTION PHENOTYPE.
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 [3] {ECO:0007744|PDB:6FU4}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 36-360 IN COMPLEX WITH HISTAMINE,
RP FUNCTION, SUBUNIT, 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).
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. TlpQ is a chemoreceptor that binds and mediates chemotaxis
CC to histamine, a key biological signaling molecule. It binds histamine
CC with high affinity, which permits responses to very low histamine
CC concentrations (PubMed:30425146). Chemotaxis to histamine may play a
CC role in the virulence of P.aeruginosa by recruiting cells at the
CC infection site and consequently modulating the expression of quorum-
CC sensing-dependent virulence genes (Probable). TlpQ also binds and
CC mediates chemotaxis to polyamines such as putrescine, spermidine,
CC cadaverine, agmatine and ethylenediamine (PubMed:30425146). In
CC addition, binds the quorum-sensing signal autoinducer 2 (AI-2), thus
CC inducing chemotaxis toward AI-2 and biofilm formation
CC (PubMed:33097715). {ECO:0000269|PubMed:30425146,
CC ECO:0000269|PubMed:33097715, ECO:0000305|PubMed:30425146}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:30425146}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: The pctABC-tlpQ deletion mutant is devoid of
CC histamine chemotaxis over the entire concentration range (50 nM to 50
CC mM) (PubMed:30425146). Deletion of the gene significantly reduces
CC chemotaxis to AI-2 (PubMed:33097715). {ECO:0000269|PubMed:30425146,
CC ECO:0000269|PubMed:33097715}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; AE004091; AAG06042.1; -; Genomic_DNA.
DR PIR; A83314; A83314.
DR RefSeq; NP_251344.1; NC_002516.2.
DR RefSeq; WP_003113383.1; NZ_QZGE01000008.1.
DR PDB; 6FU4; X-ray; 2.45 A; A/B/C/D=36-360.
DR PDBsum; 6FU4; -.
DR AlphaFoldDB; Q9I0I4; -.
DR SMR; Q9I0I4; -.
DR STRING; 287.DR97_5307; -.
DR PaxDb; Q9I0I4; -.
DR PRIDE; Q9I0I4; -.
DR EnsemblBacteria; AAG06042; AAG06042; PA2654.
DR GeneID; 882363; -.
DR KEGG; pae:PA2654; -.
DR PATRIC; fig|208964.12.peg.2777; -.
DR PseudoCAP; PA2654; -.
DR HOGENOM; CLU_000445_107_19_6; -.
DR InParanoid; Q9I0I4; -.
DR OMA; AGMEQQY; -.
DR PhylomeDB; Q9I0I4; -.
DR BioCyc; PAER208964:G1FZ6-2694-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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
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 membrane; Chemotaxis; Membrane; Methylation;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..714
FT /note="Methyl-accepting chemotaxis protein TlpQ"
FT /id="PRO_0000454655"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 50..290
FT /note="Cache"
FT /evidence="ECO:0000305"
FT DOMAIN 383..437
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 442..678
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT BINDING 170
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /evidence="ECO:0000269|PubMed:30425146,
FT ECO:0007744|PDB:6FU4"
FT BINDING 208..210
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /evidence="ECO:0000269|PubMed:30425146,
FT ECO:0007744|PDB:6FU4"
FT BINDING 239
FT /ligand="histamine"
FT /ligand_id="ChEBI:CHEBI:58432"
FT /evidence="ECO:0000269|PubMed:30425146,
FT ECO:0007744|PDB:6FU4"
FT HELIX 50..95
FT /evidence="ECO:0007829|PDB:6FU4"
FT HELIX 101..117
FT /evidence="ECO:0007829|PDB:6FU4"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:6FU4"
FT TURN 131..135
FT /evidence="ECO:0007829|PDB:6FU4"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:6FU4"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:6FU4"
FT STRAND 155..163
FT /evidence="ECO:0007829|PDB:6FU4"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:6FU4"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:6FU4"
FT HELIX 191..199
FT /evidence="ECO:0007829|PDB:6FU4"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:6FU4"
FT STRAND 215..228
FT /evidence="ECO:0007829|PDB:6FU4"
FT STRAND 231..241
FT /evidence="ECO:0007829|PDB:6FU4"
FT HELIX 242..254
FT /evidence="ECO:0007829|PDB:6FU4"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:6FU4"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:6FU4"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:6FU4"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:6FU4"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:6FU4"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:6FU4"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:6FU4"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:6FU4"
FT STRAND 314..321
FT /evidence="ECO:0007829|PDB:6FU4"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:6FU4"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:6FU4"
SQ SEQUENCE 714 AA; 77125 MW; 2FEED877F1E7ECC5 CRC64;
MFLRRLSIQW KITLLAGLCL LGVVALLVGL SVYRMQHSSV LVKSASTQML DESARLRLEA
RGELQALRIQ RYFMDAFQYG KGFSRQILFL RDQAQKRFLD AYDLREDLTR QVRTALAANP
EVLGLYVVFE PNALDGKDEL FVDQPALGSN DKGRFSLYWA QATPGQLESE SMIESELADT
SSGPSGAAYN AWYTCPKESG QPCVLDPYFD KVGERQLLMT SIAFPLELDG KVIGVMGLDI
NLSNLQALSE QGNRELYDGV GQVGILSPAG LFAGNSRDAG LLGKNLAKAD PQHAGELLQL
LAAGKSRLFN ENDDLKVLQP LQPIPGAKPW GVLLEVPKSA LLGPALALER QLDDMRREGT
WVELGLGLGA AVLGLLVLWL SARGVTRPIL GVAHMLRDIA SGEGDLTQRL PHTGRDELGE
LAGWFNRFLD KLQPIIRDVK VSVRDARSTA DQSAAISSQT SAGMQQQFRE IDQVATASHE
MTATAQDVAR SAAQAADAAR GADQATRDGL ALIDRTTQSI DSLAANLTSA MGQVEQLASS
SEEIGSVLEV IRAIAEQTNL LALNAAIEAA RAGDAGRGFA VVADEVRNLA RRTQDSVEQI
RGVIEGLQQG TRDVVDAMHG SHRQAQGSVE QVDEAVAALQ RIGEAVTVIN DMNLQIASAA
EEQSSVAEEI NRNVAAIRDV TESLSSQAEE SAQVSQSLNR LANHQQGLME QFKA
