ID   CHER_THEMA              Reviewed;         282 AA.
AC   Q9WYT5;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Chemotaxis protein methyltransferase;
DE            EC=2.1.1.80;
GN   Name=cheR; OrderedLocusNames=TM_0464;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
CC   -!- FUNCTION: Methylation of the membrane-bound methyl-accepting chemotaxis
CC       proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
CC       {ECO:0000250}.
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; AE000512; AAD35548.1; -; Genomic_DNA.
DR   PIR; H72373; H72373.
DR   RefSeq; NP_228274.1; NC_000853.1.
DR   RefSeq; WP_004081502.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9WYT5; -.
DR   SMR; Q9WYT5; -.
DR   STRING; 243274.THEMA_02370; -.
DR   DNASU; 897495; -.
DR   EnsemblBacteria; AAD35548; AAD35548; TM_0464.
DR   KEGG; tma:TM0464; -.
DR   eggNOG; COG1352; Bacteria.
DR   InParanoid; Q9WYT5; -.
DR   OMA; EWQEFVN; -.
DR   OrthoDB; 1378151at2; -.
DR   Proteomes; UP000008183; 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; 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   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00138; MeTrc; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS50123; CHER; 1.
PE   3: Inferred from homology;
KW   Chemotaxis; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..282
FT                   /note="Chemotaxis protein methyltransferase"
FT                   /id="PRO_0000176040"
FT   DOMAIN          17..282
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT   BINDING         91
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         210..211
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         226..227
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   282 AA;  34225 MW;  F3D5910026E9E0B0 CRC64;
     MQEERSEKKI GPFKFQSNFE WKEFPQEEFE WFVKEVEKRF GLNLSSYKPQ RVKRRTELLL
     RKYNVGYREY LNMLIKDKKY LDEFMDKMTI NVTEFFRNPE KWWELRDEII PLIAKNSLRM
     KFWSAGCSSG EEPYSLAILV HELNLSYKTR ILATDIDIGV LRRAQEGIYE ERAFVSTPKE
     YLEKYFEKLP DGRYRIKDSV KKIVEFKRHD LLKDPFEKNF DLIVCRNVVI YFEPEAKNEL
     YRKFAESLKP GGFLFVGNTE RIFNYKELGF EIYKPFIYRK VK