ID   CHER_CAMJJ              Reviewed;         262 AA.
AC   A1VZQ6; P45676; Q9PP10;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Chemotaxis protein methyltransferase;
DE            EC=2.1.1.80;
GN   Name=cheR; OrderedLocusNames=CJJ81176_0930;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8360165; DOI=10.1016/s0021-9258(17)46689-0;
RA   Pei Z., Blaser M.J.;
RT   "PEB1, the major cell-binding factor of Campylobacter jejuni, is a homolog
RT   of the binding component in Gram-negative nutrient transport systems.";
RL   J. Biol. Chem. 268:18717-18725(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA02917.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L13662; AAA02917.1; ALT_FRAME; Unassigned_DNA.
DR   EMBL; CP000538; EAQ71848.1; -; Genomic_DNA.
DR   RefSeq; WP_002865901.1; NC_008787.1.
DR   AlphaFoldDB; A1VZQ6; -.
DR   SMR; A1VZQ6; -.
DR   STRING; 354242.CJJ81176_0930; -.
DR   EnsemblBacteria; EAQ71848; EAQ71848; CJJ81176_0930.
DR   KEGG; cjj:CJJ81176_0930; -.
DR   eggNOG; COG1352; Bacteria.
DR   HOGENOM; CLU_025854_0_1_7; -.
DR   OMA; MWQLNAD; -.
DR   Proteomes; UP000000646; 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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..262
FT                   /note="Chemotaxis protein methyltransferase"
FT                   /id="PRO_0000281898"
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"
FT   CONFLICT        132
FT                   /note="I -> V (in Ref. 1; AAA02917)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   262 AA;  30669 MW;  4F164F8A18304328 CRC64;
     MEKKITPSEL ELNEFIKIIN EMSGIDLTDK KNILALKLNK FLEGTNTKNF SEFLGKLKSN
     RQLKQETLDF VTIGETYFLR ELAQLKEIIY YAKSLEKRVN ILSAPCSSGE EVYSLALLAA
     QNFIKDMYIL GIDINSSVIE KAKLGKYQGR TLQRLSESEK RRFFLESEDK FYTINKNELC
     TCKFELCNVF EEKFSRLGKF DIIASRNMII YFDHESKLKL MERFHRILND KGRLYVGNAD
     LIPETIYFKK IFSPRGVYYE KV