ID   CHER_LISMO              Reviewed;         262 AA.
AC   Q9XDE8;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Chemotaxis protein methyltransferase;
DE            EC=2.1.1.80;
GN   Name=cheR; OrderedLocusNames=lmo0683;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LO28 / Serovar 1/2c;
RX   PubMed=9868779; DOI=10.1111/j.1574-6968.1998.tb13338.x;
RA   Michel E., Mengaud J., Galsworthy S., Cossart P.;
RT   "Characterization of a large motility gene cluster containing the cheR,
RT   motAB genes of Listeria monocytogenes and evidence that PrfA downregulates
RT   motility genes.";
RL   FEMS Microbiol. Lett. 169:341-347(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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; AF074971; AAD41658.1; -; Genomic_DNA.
DR   EMBL; AL591976; CAC98761.1; -; Genomic_DNA.
DR   PIR; AC1160; AC1160.
DR   RefSeq; NP_464210.1; NC_003210.1.
DR   RefSeq; WP_003721803.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q9XDE8; -.
DR   SMR; Q9XDE8; -.
DR   STRING; 169963.lmo0683; -.
DR   PaxDb; Q9XDE8; -.
DR   EnsemblBacteria; CAC98761; CAC98761; CAC98761.
DR   GeneID; 985031; -.
DR   KEGG; lmo:lmo0683; -.
DR   PATRIC; fig|169963.11.peg.704; -.
DR   eggNOG; COG1352; Bacteria.
DR   HOGENOM; CLU_025854_1_1_9; -.
DR   OMA; EWQEFVN; -.
DR   PhylomeDB; Q9XDE8; -.
DR   BioCyc; LMON169963:LMO0683-MON; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..262
FT                   /note="Chemotaxis protein methyltransferase"
FT                   /id="PRO_0000176036"
FT   DOMAIN          1..262
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT   BINDING         72
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
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         191..192
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         207..208
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   262 AA;  30820 MW;  80CA858904313F2D CRC64;
     MIPDLEKDYL YFTRVVKRDL GLDLALYKET QMKRRILSFI VKKKYITFGE FFKHLKKDAV
     LLDEFISLIT INVSSFFRNR NRWDALEKQV LPRLLEDSRG KLRVWSAACS SGEEPYSLAM
     MMERSVGTRH YDILATDLEP AILKRAVIGE YQSRQMEELS EQERHTAFVE KGDTYQILPK
     YRKSIRFRRH DLLTDYYEKG FDLIVCRNVL IYFTAEGKHQ AYQKFAESLR RGGVLFIGGS
     EQILNPADYG LATLNNFFYI KT