MCPG_PSEPK
ID MCPG_PSEPK Reviewed; 624 AA.
AC Q88N45;
DT 30-NOV-2016, 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 McpG {ECO:0000305};
GN Name=mcpG {ECO:0000303|PubMed:25921834};
GN Synonyms=pctA {ECO:0000312|EMBL:AAN66994.1};
GN OrderedLocusNames=PP_1371 {ECO:0000312|EMBL:AAN66994.1};
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 GABA CHEMORECEPTOR, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=25921834; DOI=10.1111/mmi.13045;
RA Reyes-Darias J.A., Garcia V., Rico-Jimenez M., Corral-Lugo A.,
RA Lesouhaitier O., Juarez-Hernandez D., Yang Y., Bi S., Feuilloley M.,
RA Munoz-Rojas J., Sourjik V., Krell T.;
RT "Specific gamma-aminobutyrate chemotaxis in pseudomonads with different
RT lifestyle.";
RL Mol. Microbiol. 97:488-501(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. McpG is a specific gamma-aminobutyric acid (GABA)
CC chemoreceptor that recognizes GABA over a wide range of environmental
CC conditions. Contributes to attraction to and colonization of plant
CC roots. {ECO:0000269|PubMed:25921834, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene causes significant reduction
CC in GABA chemotaxis and reduces root colonization.
CC {ECO:0000269|PubMed:25921834}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; AE015451; AAN66994.1; -; Genomic_DNA.
DR RefSeq; NP_743530.1; NC_002947.4.
DR RefSeq; WP_010952482.1; NC_002947.4.
DR AlphaFoldDB; Q88N45; -.
DR SMR; Q88N45; -.
DR STRING; 160488.PP_1371; -.
DR EnsemblBacteria; AAN66994; AAN66994; PP_1371.
DR KEGG; ppu:PP_1371; -.
DR PATRIC; fig|160488.4.peg.1454; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_19_6; -.
DR OMA; TEPYIDM; -.
DR PhylomeDB; Q88N45; -.
DR BioCyc; PPUT160488:G1G01-1461-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; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029151; Sensor-like_sf.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF103190; SSF103190; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chemotaxis; Membrane; Methylation; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..624
FT /note="Methyl-accepting chemotaxis protein McpG"
FT /id="PRO_0000438505"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 36..254
FT /note="Cache"
FT /evidence="ECO:0000255"
FT DOMAIN 293..347
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 352..588
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
SQ SEQUENCE 624 AA; 67653 MW; F00C839F22076F14 CRC64;
MNKSLRFSHK ILLAASLIVI LAFSLFTLYN DYLQRNAIRE DLENYLAEMG ASTSTNIRNL
FEGRIKLVEN LAQNIAQDPA NAETLMGQNA LISSFLTVYL GKVDGGFSVR PDAKMPDGYD
PRTRPWYKDG MNASGATLTE PYIDMTTNKM VIGILSKVSS SVGVVGGDLA LDGLVQIINS
LNFGGMGYAF LVNDQGKILV HPDKDLVMKS LSDLFPQHTP KLTGELTEVQ SDGQTRLLTF
SPITGLPSAN WYIGLSVDKD KAFSMLSTFR TSAVIATVVA VVIIIGLLGL LIRVLMQPLH
TMTRAMEDIA EGEGDLTKRL HIHSHDEFGV LGNAFNRFVE RIHSSIREVS SATEQVNEVA
LRVISASNSS MTNSDEQSNR TNSVAAAINE LGAAAQEIAG NAAQASQHAS SARLLAEEGQ
QVVERNIAAM NRLSDLIVTS SAHIETLNSK TVNIGQILEV ITSISQQTNL LALNAAIEAA
RAGEAGRGFA VVADEVRNLA HRTQESAQQV QTMIEELQVG ARESVDTMEQ SQRHSQDSMQ
IANQAGERLD SVTVRIGEID GMNQSVATAT EEQTAVVEAI NMDINEINML NQEGVENLQA
TLRACSDLEQ QAGRLKHLVG SFRI
