ID   CHER3_PSEPK             Reviewed;         273 AA.
AC   Q88GG4;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Putative methyltransferase Cher3;
DE            EC=2.1.1.-;
GN   Name=cheR3; OrderedLocusNames=PP_3760;
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   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   -!- DISRUPTION PHENOTYPE: Mutation does not affect chemotaxis and biofilm
CC       formation. {ECO:0000269|PubMed:23677992}.
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DR   EMBL; AE015451; AAN69354.1; -; Genomic_DNA.
DR   RefSeq; NP_745890.1; NC_002947.4.
DR   RefSeq; WP_010954591.1; NC_002947.4.
DR   AlphaFoldDB; Q88GG4; -.
DR   SMR; Q88GG4; -.
DR   STRING; 160488.PP_3760; -.
DR   EnsemblBacteria; AAN69354; AAN69354; PP_3760.
DR   KEGG; ppu:PP_3760; -.
DR   PATRIC; fig|160488.4.peg.4010; -.
DR   eggNOG; COG1352; Bacteria.
DR   HOGENOM; CLU_025854_1_0_6; -.
DR   OMA; DYYTAAY; -.
DR   PhylomeDB; Q88GG4; -.
DR   BioCyc; PPUT160488:G1G01-4013-MON; -.
DR   BRENDA; 2.1.1.80; 5092.
DR   Proteomes; UP000000556; Chromosome.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR022642; CheR_C.
DR   InterPro; IPR000780; CheR_MeTrfase.
DR   InterPro; IPR022641; CheR_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01739; CheR; 1.
DR   Pfam; PF03705; CheR_N; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00138; MeTrc; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS50123; CHER; 1.
PE   4: Predicted;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..273
FT                   /note="Putative methyltransferase Cher3"
FT                   /id="PRO_0000424794"
FT   DOMAIN          1..273
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT   BINDING         76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..200
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         215..216
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   273 AA;  31647 MW;  89CB74822690B142 CRC64;
     MTSERNTDIE IRLLIEAIYL KYSYDFRNYS GASIKRRILH ALRQFDCLTV SALQERVLHD
     PGMFMQLLQY LTIPVSEMFR DPDHFLAVRN EVVPLLRTWP SIKVWIAGCS TGEEVYSMAI
     LLREEGLLER TIIYATDINP HSLDRAKQGI YSMQSMREYE ENYRLAGGRR DFAEYYTAAY
     GNAIMDSSLR DNVTFADHSL ATDSVFSETQ LVSCRNVLIY FNKDLQDRAL GLFHESLCHR
     GFLVLGSKES VDFSAYSDRF EPLVKPQRIF RKS