MCPS_PSEPK
ID MCPS_PSEPK Reviewed; 639 AA.
AC Q88E10;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Methyl-accepting chemotaxis protein McpS;
GN Name=mcpS; OrderedLocusNames=PP_4658;
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, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=20498372; DOI=10.1074/jbc.m110.110403;
RA Lacal J., Alfonso C., Liu X., Parales R.E., Morel B., Conejero-Lara F.,
RA Rivas G., Duque E., Ramos J.L., Krell T.;
RT "Identification of a chemoreceptor for tricarboxylic acid cycle
RT intermediates: differential chemotactic response towards receptor
RT ligands.";
RL J. Biol. Chem. 285:23126-23136(2010).
RN [3]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=21360620; DOI=10.1002/jmr.1101;
RA Lacal J., Garcia-Fontana C., Callejo-Garcia C., Ramos J.L., Krell T.;
RT "Physiologically relevant divalent cations modulate citrate recognition by
RT the McpS chemoreceptor.";
RL J. Mol. Recognit. 24:378-385(2011).
RN [4]
RP METHYLATION BY CHER2.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=23677992; DOI=10.1074/jbc.m113.472605;
RA Garcia-Fontana C., Reyes-Darias J.A., Munoz-Martinez F., Alfonso C.,
RA Morel B., Ramos J.L., Krell T.;
RT "High specificity in CheR methyltransferase function: CheR2 of Pseudomonas
RT putida is essential for chemotaxis, whereas CheR1 is involved in biofilm
RT formation.";
RL J. Biol. Chem. 288:18987-18999(2013).
RN [5]
RP CRYSTALLIZATION OF 47-283.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=22505412; DOI=10.1107/s1744309112004940;
RA Gavira J.A., Lacal J., Ramos J.L., Garcia-Ruiz J.M., Krell T.,
RA Pineda-Molina E.;
RT "Crystallization and crystallographic analysis of the ligand-binding domain
RT of the Pseudomonas putida chemoreceptor McpS in complex with malate and
RT succinate.";
RL Acta Crystallogr. F 68:428-431(2012).
RN [6] {ECO:0007744|PDB:2YFA, ECO:0007744|PDB:2YFB}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 46-283 IN COMPLEX WITH
RP (S)-MALATE; SUCCINATE AND ACETATE, SUBUNIT, AND MUTAGENESIS OF ARG-60;
RP ARG-63; ARG-183 AND ARG-254.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=23112148; DOI=10.1073/pnas.1201400109;
RA Pineda-Molina E., Reyes-Darias J.A., Lacal J., Ramos J.L.,
RA Garcia-Ruiz J.M., Gavira J.A., Krell T.;
RT "Evidence for chemoreceptors with bimodular ligand-binding regions
RT harboring two signal-binding sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18926-18931(2012).
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. McpS is a specific chemoreceptor for 6 tricarboxylic acid
CC (TCA) cycle intermediates (succinate, fumarate, malate, oxaloacetate,
CC citrate and isocitrate), butyrate and acetate. Malate, succinate,
CC fumarate and oxaloacetate cause the strongest chemotactic response.
CC {ECO:0000269|PubMed:20498372, ECO:0000269|PubMed:21360620}.
CC -!- ACTIVITY REGULATION: Binding of citrate to the ligand-binding domain
CC reduces the chemotaxis towards the strong attractants such as malate
CC and succinate. However, in physiologically relevant niches, citrate is
CC mostly complexed with magnesium or calcium ions, and does not bind
CC McpS. {ECO:0000269|PubMed:21360620}.
CC -!- SUBUNIT: Homodimer. Exists as a mixture of monomers and dimers in
CC solution. Ligand binding stabilizes the dimeric form.
CC {ECO:0000269|PubMed:20498372, ECO:0000269|PubMed:23112148}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Methylated by CheR2. {ECO:0000269|PubMed:23677992}.
CC -!- DISRUPTION PHENOTYPE: Mutant fails to respond to succinate but responds
CC to toluene. {ECO:0000269|PubMed:20498372}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; AE015451; AAN70231.1; -; Genomic_DNA.
DR RefSeq; NP_746767.1; NC_002947.4.
DR RefSeq; WP_010955314.1; NC_002947.4.
DR PDB; 2YFA; X-ray; 1.80 A; A/B=46-283.
DR PDB; 2YFB; X-ray; 1.90 A; A/B=46-283.
DR PDBsum; 2YFA; -.
DR PDBsum; 2YFB; -.
DR AlphaFoldDB; Q88E10; -.
DR SMR; Q88E10; -.
DR DIP; DIP-60088N; -.
DR STRING; 160488.PP_4658; -.
DR EnsemblBacteria; AAN70231; AAN70231; PP_4658.
DR KEGG; ppu:PP_4658; -.
DR PATRIC; fig|160488.4.peg.4966; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_27_6; -.
DR OMA; IDRSNWM; -.
DR PhylomeDB; Q88E10; -.
DR BioCyc; PPUT160488:G1G01-4971-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; IPR032255; HBM.
DR InterPro; IPR004089; MCPsignal_dom.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF16591; HBM; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM01358; HBM; 1.
DR SMART; SM00283; MA; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS51753; HBM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chemotaxis; Coiled coil; Membrane;
KW Methylation; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..639
FT /note="Methyl-accepting chemotaxis protein McpS"
FT /id="PRO_0000424826"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..288
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..639
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..283
FT /note="HBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01089"
FT DOMAIN 310..362
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 367..603
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT COILED 191..245
FT /evidence="ECO:0000255"
FT BINDING 60..65
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000269|PubMed:23112148,
FT ECO:0007744|PDB:2YFA"
FT BINDING 60..65
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0000269|PubMed:23112148,
FT ECO:0007744|PDB:2YFB"
FT BINDING 138
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000269|PubMed:23112148,
FT ECO:0007744|PDB:2YFA, ECO:0007744|PDB:2YFB"
FT BINDING 183
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000269|PubMed:23112148,
FT ECO:0007744|PDB:2YFA, ECO:0007744|PDB:2YFB"
FT BINDING 187
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000269|PubMed:23112148,
FT ECO:0007744|PDB:2YFA, ECO:0007744|PDB:2YFB"
FT BINDING 236
FT /ligand="acetate"
FT /ligand_id="ChEBI:CHEBI:30089"
FT /evidence="ECO:0000269|PubMed:23112148,
FT ECO:0007744|PDB:2YFA, ECO:0007744|PDB:2YFB"
FT BINDING 254
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000269|PubMed:23112148,
FT ECO:0007744|PDB:2YFA"
FT BINDING 254
FT /ligand="succinate"
FT /ligand_id="ChEBI:CHEBI:30031"
FT /evidence="ECO:0000269|PubMed:23112148,
FT ECO:0007744|PDB:2YFB"
FT BINDING 258
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000269|PubMed:23112148,
FT ECO:0007744|PDB:2YFA"
FT MUTAGEN 60
FT /note="R->A: Abolishes binding of malate, fumarate,
FT oxaloacetate, succinate, isocitrate and butyrate. Decreases
FT binding of citrate."
FT /evidence="ECO:0000269|PubMed:23112148"
FT MUTAGEN 63
FT /note="R->A: Abolishes binding of malate, fumarate,
FT oxaloacetate, succinate, isocitrate and butyrate. Decreases
FT binding of citrate."
FT /evidence="ECO:0000269|PubMed:23112148"
FT MUTAGEN 183
FT /note="R->A: Decreases binding of acetate. Does not affect
FT binding of malate."
FT /evidence="ECO:0000269|PubMed:23112148"
FT MUTAGEN 254
FT /note="R->A: Abolishes binding of malate, fumarate,
FT oxaloacetate, succinate and isocitrate. Decreases binding
FT of citrate. Does not affect binding of butyrate."
FT /evidence="ECO:0000269|PubMed:23112148"
FT HELIX 46..68
FT /evidence="ECO:0007829|PDB:2YFA"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2YFA"
FT HELIX 73..96
FT /evidence="ECO:0007829|PDB:2YFA"
FT HELIX 100..157
FT /evidence="ECO:0007829|PDB:2YFA"
FT HELIX 162..191
FT /evidence="ECO:0007829|PDB:2YFA"
FT HELIX 195..218
FT /evidence="ECO:0007829|PDB:2YFA"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2YFA"
FT HELIX 223..276
FT /evidence="ECO:0007829|PDB:2YFA"
SQ SEQUENCE 639 AA; 68764 MW; 827C3ADD979A87DB CRC64;
MNSWFANISV NLKLGLGFGL VLVLTGLLAL TGWTSLGSLI DRSNWMGDIG QLNKDLTDLR
IARLQYMIAN GDDTAAANTL AKLDAFSKQQ AYLATTFKSP ENVKLLGELG DTISAYKLSL
NKMRQGYDAT RAARVSMDSS AIRADQAMDA LSQEVMARPE ADSVRLAQYQ LISKARQQLL
QVRIDVRGYI AENSSANEQA ALRQLDAALA DTDNLKRQLP SEDARLQQFE NAVLAYRDAV
RQFRDAVANI TTSRAEMTVQ GADIVKRSDA LYQIQLERRD IESTQARSLQ AIATLLALLV
GVLAAVLITR QITRPLQDTL VAVEKIASGD LTQHMRVTRR DELGVLQQGI ARMGTTLREL
ISGIRDGVTQ IASAAEELSA VTEQTSAGAN SQKVETDQVA TAMHEMAATV QEVARNAEQA
SHAATGADDE ARAGDRVVGE AIGQIERLAE DMHRSTEAMN LLQQESQKIG SVMDVIKSVA
EQTNLLALNA AIEAARAGEA GRGFAVVADE VRGLAQRTQK STEEIEELIA SLQHGTQQVA
NAMQGSRALT DSSVELARKA GSSLESITST VSSIQSMNQQ IAAAAEQQSA VAEEISRSIL
NVRDVSEQTA AASDETAASS VELARLGGQL QTLVSQFRV
