MCPQ_PSEPK
ID MCPQ_PSEPK Reviewed; 638 AA.
AC Q88D09;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Methyl-accepting chemotaxis protein McpQ {ECO:0000305};
GN Name=mcpQ {ECO:0000303|PubMed:26463109};
GN OrderedLocusNames=PP_5020 {ECO:0000312|EMBL:AAN70585.1};
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=26463109; DOI=10.1111/1462-2920.13030;
RA Martin-Mora D., Reyes-Darias J.A., Ortega A., Corral-Lugo A., Matilla M.A.,
RA Krell T.;
RT "McpQ is a specific citrate chemoreceptor that responds preferentially to
RT citrate/metal ion complexes.";
RL Environ. Microbiol. 18:3284-3295(2016).
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. McpQ recognizes specifically citrate and citrate/metal(2+)
CC complexes. Binds citrate/metal(2+) complexes with higher affinity than
CC free citrate, and mediates preferentially chemotaxis toward
CC citrate/metal(2+) complexes. {ECO:0000269|PubMed:26463109,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene causes very strong reduction
CC in the chemotaxis toward citrate/Mg(2+) complexes.
CC {ECO:0000269|PubMed:26463109}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; AE015451; AAN70585.1; -; Genomic_DNA.
DR RefSeq; NP_747121.1; NC_002947.4.
DR RefSeq; WP_010955579.1; NC_002947.4.
DR AlphaFoldDB; Q88D09; -.
DR SMR; Q88D09; -.
DR STRING; 160488.PP_5020; -.
DR EnsemblBacteria; AAN70585; AAN70585; PP_5020.
DR KEGG; ppu:PP_5020; -.
DR PATRIC; fig|160488.4.peg.5361; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_27_6; -.
DR OMA; ANINQYQ; -.
DR PhylomeDB; Q88D09; -.
DR BioCyc; PPUT160488:G1G01-5365-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; IPR032255; HBM.
DR InterPro; IPR004089; MCPsignal_dom.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF16591; HBM; 1.
DR Pfam; PF00015; MCPsignal; 1.
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 Cell membrane; Chemotaxis; Membrane; Methylation; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..638
FT /note="Methyl-accepting chemotaxis protein McpQ"
FT /id="PRO_0000438508"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 45..282
FT /note="HBM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01089"
FT DOMAIN 309..361
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 366..602
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
SQ SEQUENCE 638 AA; 69017 MW; 2FE336A2FEC83596 CRC64;
MYQWLAQSLG NVSVNRKLGL GFGLVLLLTL AITLTGWHGM DSIIDRGDKL GNISVIQQYT
QELRIARQQY DRRRDDASLA ELEKALSNLD RQVQLMLGQI EQPADHQRLE QQREAVRIYQ
QAFNELKQAD QRREASRDVL GSSADKAVDL IGRVQRSLLQ GANINQYQHA VDVSALLQQA
RFQVRGYTYS GNADYQQTAL KAIDQALAEL RALPAKVPAE HAASLDDAAT AMGGYRDAVT
QFGNAQLASE QALQRMVEQG TVLLQASQMM TASQTEVRDA AAAQAKTLLT VATVLALALG
LLAAWAITRQ IIIPLRQTLR AAERVASGDL TQSLQVQRRD ELGQLQASMH RMTQGLRELI
GGIGDGVTQI ASAAEELSAV TEQTSAGVNN QKVETDQVAT AMNQMTATVH EVARNAEQAS
EAALMADQQA REGDRVVGEA VAQIERLASE VVNSSEAMNL LKTESDKIGS VLDVIKSVAQ
QTNLLALNAA IEAARAGEAG RGFAVVADEV RSLAQRTQQS TEEIEELIAG LQSGTQRVAS
VMDNSRQLTD SSVELTRRAG SSLETITRTV SSIQAMNQQI ATAAEEQTAV AEEINRSVMN
VRDISDQTSA ASEETASSSV ELARLGTHLQ GLVGRFRL
