ID   CHER_CAMJE              Reviewed;         262 AA.
AC   Q0P9X6; P45676; Q9PP10;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Chemotaxis protein methyltransferase;
DE            EC=2.1.1.80;
GN   Name=cheR; OrderedLocusNames=Cj0923c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL35043.1; -; Genomic_DNA.
DR   PIR; B48518; B48518.
DR   PIR; B81366; B81366.
DR   RefSeq; WP_002853285.1; NC_002163.1.
DR   RefSeq; YP_002344321.1; NC_002163.1.
DR   AlphaFoldDB; Q0P9X6; -.
DR   SMR; Q0P9X6; -.
DR   IntAct; Q0P9X6; 1.
DR   STRING; 192222.Cj0923c; -.
DR   PaxDb; Q0P9X6; -.
DR   PRIDE; Q0P9X6; -.
DR   DNASU; 905222; -.
DR   EnsemblBacteria; CAL35043; CAL35043; Cj0923c.
DR   GeneID; 905222; -.
DR   KEGG; cje:Cj0923c; -.
DR   PATRIC; fig|192222.6.peg.907; -.
DR   eggNOG; COG1352; Bacteria.
DR   HOGENOM; CLU_025854_0_1_7; -.
DR   OMA; MWQLNAD; -.
DR   Proteomes; UP000000799; 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..262
FT                   /note="Chemotaxis protein methyltransferase"
FT                   /id="PRO_0000176032"
FT   DOMAIN          1..262
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         111
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         188..189
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         206..207
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   262 AA;  30655 MW;  57B545B90AA04328 CRC64;
     MEKKITPSEL ELNEFIKIIN EMSGIDLTDK KNILALKLNK FLEGTNTKNF SEFLGKLKSN
     RQLKQETLDF VTIGETYFLR ELAQLKEIIY YAKSLEKRVN ILSAPCSSGE EVYSLALLAA
     QNFIKDMYIL GVDINSSVIE KAKLGKYQGR TLQRLSESEK RRFFLESEDK FYTINKNELC
     TCKFELCNVF EEKFSRLGKF DIIASRNMII YFDHESKLKL MERFHRILND KGRLYVGNAD
     LIPETIYFKK IFSPRGVYYE KV