CHER_ECOLI
ID CHER_ECOLI Reviewed; 286 AA.
AC P07364; P78071;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Chemotaxis protein methyltransferase;
DE EC=2.1.1.80;
GN Name=cheR; Synonyms=cheX; OrderedLocusNames=b1884, JW1873;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3510184; DOI=10.1128/jb.165.1.161-166.1986;
RA Mutoh N., Simon M.I.;
RT "Nucleotide sequence corresponding to five chemotaxis genes in Escherichia
RT coli.";
RL J. Bacteriol. 165:161-166(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Methylation of the membrane-bound methyl-accepting chemotaxis
CC proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
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;
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DR EMBL; M13463; AAA23568.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74954.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15700.1; -; Genomic_DNA.
DR PIR; D64951; XYECCR.
DR RefSeq; NP_416398.1; NC_000913.3.
DR RefSeq; WP_000204337.1; NZ_LN832404.1.
DR AlphaFoldDB; P07364; -.
DR SMR; P07364; -.
DR BioGRID; 4260375; 237.
DR BioGRID; 850753; 3.
DR DIP; DIP-9273N; -.
DR IntAct; P07364; 16.
DR STRING; 511145.b1884; -.
DR PaxDb; P07364; -.
DR PRIDE; P07364; -.
DR EnsemblBacteria; AAC74954; AAC74954; b1884.
DR EnsemblBacteria; BAA15700; BAA15700; BAA15700.
DR GeneID; 946396; -.
DR KEGG; ecj:JW1873; -.
DR KEGG; eco:b1884; -.
DR PATRIC; fig|1411691.4.peg.363; -.
DR EchoBASE; EB0146; -.
DR eggNOG; COG1352; Bacteria.
DR HOGENOM; CLU_025854_0_0_6; -.
DR InParanoid; P07364; -.
DR OMA; EWQEFVN; -.
DR PhylomeDB; P07364; -.
DR BioCyc; EcoCyc:CHER-MON; -.
DR BioCyc; MetaCyc:CHER-MON; -.
DR PRO; PR:P07364; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0098561; C:methyl accepting chemotaxis protein complex; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:CAFA.
DR GO; GO:0008276; F:protein methyltransferase activity; IMP:EcoCyc.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IDA:CAFA.
DR GO; GO:0006935; P:chemotaxis; IMP:EcoCyc.
DR GO; GO:0006479; P:protein methylation; IDA:CAFA.
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 4: Predicted;
KW Chemotaxis; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..286
FT /note="Chemotaxis protein methyltransferase"
FT /id="PRO_0000176033"
FT DOMAIN 15..286
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 212..213
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 230..231
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT CONFLICT 113
FT /note="R -> G (in Ref. 1; AAA23568)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 32849 MW; 2AFA307DD406B135 CRC64;
MTSSLPCGQT SLLLQMTERL ALSDAHFRRI SQLIYQRAGI VLADHKRDMV YNRLVRRLRS
LGLTDFGHYL NLLESNQHSG EWQAFINSLT TNLTAFFREA HHFPLLADHA RRRSGEYRVW
SAAASTGEEP YSIAMTLADT LGTAPGRWKV FASDIDTEVL EKARSGIYRH EELKNLTPQQ
LQRYFMRGTG PHEGLVRVRQ ELANYVDFAP LNLLAKQYTV PGPFDAIFCR NVMIYFDQTT
QQEILRRFVP LLKPDGLLFA GHSENFSHLE RRFTLRGQTV YALSKD
