MCPU_PSEPK
ID MCPU_PSEPK Reviewed; 688 AA.
AC Q88NI1;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Methyl-accepting chemotaxis protein McpU {ECO:0000305};
GN Name=mcpU {ECO:0000303|PubMed:26662997};
GN OrderedLocusNames=PP_1228 {ECO:0000312|EMBL:AAN66852.1};
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 AS A CHEMORECEPTOR, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=26662997; DOI=10.1111/1462-2920.13170;
RA Corral-Lugo A., de la Torre J., Matilla M.A., Fernandez M., Morel B.,
RA Espinosa-Urgel M., Krell T.;
RT "Assessment of the contribution of chemoreceptor-based signaling to biofilm
RT formation.";
RL Environ. Microbiol. 18:3355-3372(2016).
RN [3]
RP FUNCTION.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 33-334 IN COMPLEX WITH
RP PUTRESCINE, DOMAIN, AND MUTAGENESIS OF GLU-164; MET-170; TRP-186; TYR-202;
RP ASP-204 AND ASP-233.
RX PubMed=29758259; DOI=10.1016/j.jmb.2018.05.008;
RA Gavira J.A., Ortega A., Martin-Mora D., Conejero-Muriel M.T.,
RA Corral-Lugo A., Morel B., Matilla M.A., Krell T.;
RT "Structural basis for polyamine binding at the dCACHE domain of the McpU
RT chemoreceptor from Pseudomonas putida.";
RL J. Mol. Biol. 430:1950-1963(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. McpU is a chemoreceptor that binds and mediates chemotaxis
CC to polyamines such as putrescine, spermidine, cadaverine and agmatine
CC (PubMed:26662997, PubMed:30425146). Also binds histamine and
CC ethylenediamine with much lower affinities (PubMed:30425146).
CC {ECO:0000269|PubMed:26662997, ECO:0000269|PubMed:30425146}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DOMAIN: The ligand binding domain (LBD) is monomeric in solution.
CC Ligand binding does not cause major conformational changes or
CC alterations in the oligomeric state of the LBD.
CC {ECO:0000269|PubMed:29758259}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows increased biofilm formation as
CC compared to the wild type. Mutation decreases plant root colonization.
CC {ECO:0000269|PubMed:26662997}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; AE015451; AAN66852.1; -; Genomic_DNA.
DR RefSeq; NP_743388.1; NC_002947.4.
DR RefSeq; WP_010952371.1; NC_002947.4.
DR PDB; 6F9G; X-ray; 2.39 A; A/B/C/D/E=33-334.
DR PDBsum; 6F9G; -.
DR AlphaFoldDB; Q88NI1; -.
DR SMR; Q88NI1; -.
DR STRING; 160488.PP_1228; -.
DR EnsemblBacteria; AAN66852; AAN66852; PP_1228.
DR KEGG; ppu:PP_1228; -.
DR PATRIC; fig|160488.4.peg.1304; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_19_6; -.
DR OMA; FAGYMVW; -.
DR PhylomeDB; Q88NI1; -.
DR BioCyc; PPUT160488:G1G01-1314-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: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..688
FT /note="Methyl-accepting chemotaxis protein McpU"
FT /id="PRO_0000438509"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 50..284
FT /note="Cache"
FT /evidence="ECO:0000305"
FT DOMAIN 357..411
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 416..652
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT BINDING 202..204
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000269|PubMed:29758259,
FT ECO:0007744|PDB:6F9G"
FT BINDING 233
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000269|PubMed:29758259,
FT ECO:0007744|PDB:6F9G"
FT MUTAGEN 164
FT /note="E->A: 20-fold decrease in affinity for putrescine.
FT 7-fold decrease in affinity for spermidine. Increases
FT affinity for cadaverine."
FT /evidence="ECO:0000269|PubMed:29758259"
FT MUTAGEN 170
FT /note="M->A: Does not bind putrescine. Does not affect
FT affinity for spermidine. 3-fold decrease in affinity for
FT cadaverine."
FT /evidence="ECO:0000269|PubMed:29758259"
FT MUTAGEN 186
FT /note="W->A: Does not bind putrescine. 100-fold decrease in
FT affinity for spermidine. 36-fold decrease in affinity for
FT cadaverine."
FT /evidence="ECO:0000269|PubMed:29758259"
FT MUTAGEN 202
FT /note="Y->A: Does not bind putrescine. 24-fold decrease in
FT affinity for spermidine. 16-fold decrease in affinity for
FT cadaverine."
FT /evidence="ECO:0000269|PubMed:29758259"
FT MUTAGEN 204
FT /note="D->A: Does not bind putrescine and spermidine. 12-
FT fold decrease in affinity for cadaverine."
FT /evidence="ECO:0000269|PubMed:29758259"
FT MUTAGEN 233
FT /note="D->A: Does not bind putrescine, spermidine and
FT cadaverine."
FT /evidence="ECO:0000269|PubMed:29758259"
FT HELIX 55..93
FT /evidence="ECO:0007829|PDB:6F9G"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:6F9G"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:6F9G"
FT TURN 125..129
FT /evidence="ECO:0007829|PDB:6F9G"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:6F9G"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:6F9G"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:6F9G"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:6F9G"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:6F9G"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:6F9G"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:6F9G"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:6F9G"
FT STRAND 209..222
FT /evidence="ECO:0007829|PDB:6F9G"
FT STRAND 225..235
FT /evidence="ECO:0007829|PDB:6F9G"
FT HELIX 236..249
FT /evidence="ECO:0007829|PDB:6F9G"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:6F9G"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:6F9G"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:6F9G"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:6F9G"
FT STRAND 286..295
FT /evidence="ECO:0007829|PDB:6F9G"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:6F9G"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:6F9G"
SQ SEQUENCE 688 AA; 73694 MW; BBBE993BF75BB300 CRC64;
MPLRRLSIQW KITLLAGLCL LAIVALLVAT SLTQAHRSAA LVNQANTAML EDSARQRLQA
HAETQALRIQ RYFMDAYQYG NGFARLVQVL KDRGGSDLRA ELTRQARASL AGNPDVIGLY
LVFQPNALDQ QDSHYLGQDA MGSNESGRFS LYWSQPSPGT LELEAMPETM LGDTSIGSNG
AAKNRWLTCP QDTARTCMLE PYLDEVNGRQ VLMTSIALPL LEHGKVVGVV GLDIGLANLQ
QLSVNGRRDL FDGQGQVSIA TAAGLLAGNS RDDSVLGKPM DKSVADGLLR VAHPFTPIPD
TAPWQVVLEL PESVLQAPAV ALNQRLDAHN QNANLTSLLI GLGTAIAGLL LVWLTARGVT
RPILAVAARL EDIASGEGDL TRRLDYAHQD ELGQLTGWFN RFLDKLQPVI AQVKGSLQEA
RNTADQSAAI ASQTSDGMQQ QHREIEQVAT AANEMSATAL DVAHNASQAA QAARAADQAS
QEGLQLVDST RQGIDRLAAG MNTAMDEARA LEDRSGQIGS VLEVIRTIAE QTNLLALNAA
IEAARAGEAG RGFAVVADEV RGLAQRTQVS VEEIRQVIEG LQQGTQDVVG AMHAGQRQAQ
DSAARMEQAL PALQRIGEAV AVISDMNLQI ASAAEEQSAV AEEVNRNVAG IRDVTESLAG
QADESARISQ ALNRLANQQQ ALMEQFRV
