CHER2_PSEPK
ID CHER2_PSEPK Reviewed; 275 AA.
AC Q88ER1;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Chemotaxis protein methyltransferase Cher2;
DE EC=2.1.1.80;
GN Name=cheR2; OrderedLocusNames=PP_4392;
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=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).
CC -!- FUNCTION: Methylation of the membrane-bound methyl-accepting chemotaxis
CC proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
CC Methylates the McpS chemotaxis receptor. {ECO:0000269|PubMed:23677992}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; EC=2.1.1.80;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23677992}.
CC -!- DISRUPTION PHENOTYPE: Mutants are deficient in chemotaxis toward malate
CC and casamino acids. Mutation does not affect biofilm formation.
CC {ECO:0000269|PubMed:23677992}.
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DR EMBL; AE015451; AAN69970.1; -; Genomic_DNA.
DR RefSeq; NP_746506.1; NC_002947.4.
DR RefSeq; WP_004575768.1; NC_002947.4.
DR AlphaFoldDB; Q88ER1; -.
DR SMR; Q88ER1; -.
DR STRING; 160488.PP_4392; -.
DR PRIDE; Q88ER1; -.
DR EnsemblBacteria; AAN69970; AAN69970; PP_4392.
DR GeneID; 66677026; -.
DR KEGG; ppu:PP_4392; -.
DR PATRIC; fig|160488.4.peg.4667; -.
DR eggNOG; COG1352; Bacteria.
DR HOGENOM; CLU_025854_0_2_6; -.
DR OMA; PGIIYKA; -.
DR PhylomeDB; Q88ER1; -.
DR BioCyc; PPUT160488:G1G01-4670-MON; -.
DR BRENDA; 2.1.1.80; 5092.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.155.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR026024; Chemotaxis_MeTrfase_CheR.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR036804; CheR_N_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR PIRSF; PIRSF000410; CheR; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00138; MeTrc; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS50123; CHER; 1.
PE 1: Evidence at protein level;
KW Chemotaxis; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..275
FT /note="Chemotaxis protein methyltransferase Cher2"
FT /id="PRO_0000424793"
FT DOMAIN 1..275
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 201..202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 218..219
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 275 AA; 31084 MW; AFC93E08C4BDBE50 CRC64;
MSTGNLDFEQ FRVFLEKACG ILLGENKQYL VSSRLNKLME QQGIKSLGEL VQRIQAQPRG
GLREQVVDAM TTNETLWFRD TYPFEVLKNK VIPEFIRNNP GQRLRMWSAA CSSGQEPYSI
SMAIDEFERS NLGQLKMGAQ IVATDLSGTM LTNCKTGEYD SLAIARGLSQ ERLQRYFDPK
GPGRWAVKPA IRSRVEFRSF NLLDSYASLG KFDIVFCRNV LIYFSAQVKK DILLRIHSTL
KPGGYLFLGA SEALNGLPDH YQMVQCSPGI IYQAK
