ID   CHER_VIBAN              Reviewed;         275 AA.
AC   Q57508;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Chemotaxis protein methyltransferase;
DE            EC=2.1.1.80;
GN   Name=cheR;
OS   Vibrio anguillarum (Listonella anguillarum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=55601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NB10 / Serotype O1;
RX   PubMed=8830252; DOI=10.1046/j.1365-2958.1996.412927.x;
RA   O'Toole R., Milton D.L., Wolf-Watz H.;
RT   "Chemotactic motility is required for invasion of the host by the fish
RT   pathogen Vibrio anguillarum.";
RL   Mol. Microbiol. 19:625-637(1996).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U36378; AAB38489.1; -; Genomic_DNA.
DR   PIR; S70895; S70895.
DR   RefSeq; WP_013856250.1; NZ_VSLF01000002.1.
DR   AlphaFoldDB; Q57508; -.
DR   SMR; Q57508; -.
DR   STRING; 55601.VANGNB10_cI1998c; -.
DR   GeneID; 63946338; -.
DR   OMA; PGIIYKA; -.
DR   OrthoDB; 1378151at2; -.
DR   GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
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   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..275
FT                   /note="Chemotaxis protein methyltransferase"
FT                   /id="PRO_0000176041"
FT   DOMAIN          1..275
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         78
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         201..202
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         218..219
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   275 AA;  30809 MW;  0A44C10F0C5D9C53 CRC64;
     MTAITISDQE YRDFSRFLES QCGIVLGDSK QYLVRSRLSP LVAKFKLTSL SDLLRDVVTG
     RNRELRVAAV DAMTTNETLW FRDAYPFTVL AERLLPEVAA NKRPIKIWSA ASSSGQEPYS
     MAMTVLETQQ RKPGMLPSVA ITATDISASM LDMCKAGIYD NLALGRGLSP ERRKIFFEDA
     GDGRMKIKDN VKRLVNFRPQ NLMESYALLG KFDIIFCRNV LIYFSPDMKS KVLNQMASSL
     NPGGYLLLGA SESLTGLTDK FEMVRCNPGI IYKLK