ID   CHER2_VIBCH             Reviewed;         288 AA.
AC   Q9KS61;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Chemotaxis protein methyltransferase 2;
DE            EC=2.1.1.80;
GN   Name=cheR2; OrderedLocusNames=VC_1399;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(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; AE003852; AAF94556.1; -; Genomic_DNA.
DR   PIR; G82205; G82205.
DR   RefSeq; NP_231042.1; NC_002505.1.
DR   RefSeq; WP_001002908.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KS61; -.
DR   SMR; Q9KS61; -.
DR   STRING; 243277.VC_1399; -.
DR   DNASU; 2614031; -.
DR   EnsemblBacteria; AAF94556; AAF94556; VC_1399.
DR   KEGG; vch:VC_1399; -.
DR   PATRIC; fig|243277.26.peg.1330; -.
DR   eggNOG; COG1352; Bacteria.
DR   HOGENOM; CLU_025854_0_1_6; -.
DR   OMA; GKMDVIF; -.
DR   BioCyc; VCHO:VC1399-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
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; IPR026024; Chemotaxis_MeTrfase_CheR.
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   PIRSF; PIRSF000410; CheR; 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..288
FT                   /note="Chemotaxis protein methyltransferase 2"
FT                   /id="PRO_0000176043"
FT   DOMAIN          1..280
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         119
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         200..201
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         219..220
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   288 AA;  33631 MW;  84CFE420653B7300 CRC64;
     MNEIVITDTD FCRFRDYFYQ KTGIFFENSK RYFVDKRLLQ RIELTEHQSF RGYFTYLRFQ
     ASGEELQAVI NALTVNETYF FREISQLESL VEEVLDDIVR HRPGELIRIW SMPCSSGEEP
     YSIVLFLLEH WPKLEQVDIE IIASDIDTGI LQKAAQGIFS ARSVKNLPNS SLNKYFSLRA
     DGSYQLIDDI RQSVRFTQTN LNNRAEVQKL GAMDVIFCRN LLIYFDDISR RNAVESFYEQ
     LNPGGVLFLG HSESMSRISS IFHVKRFRKS TGYYKPHKGK SDEKSNGR