ID   CHER_HALS3              Reviewed;         268 AA.
AC   B0R4J5;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Chemotaxis protein methyltransferase;
DE            EC=2.1.1.80;
DE   AltName: Full=Protein-glutamate O-methyltransferase CheR;
GN   Name=cheR; OrderedLocusNames=OE_2406R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=R1 / S9;
RX   PubMed=18514223; DOI=10.1016/j.jmb.2008.04.063;
RA   Koch M.K., Staudinger W.F., Siedler F., Oesterhelt D.;
RT   "Physiological sites of deamidation and methyl esterification in sensory
RT   transducers of Halobacterium salinarum.";
RL   J. Mol. Biol. 380:285-302(2008).
CC   -!- FUNCTION: Catalyzes the methylation of several Htr transducer proteins
CC       (methyl-accepting chemotaxis proteins) to form gamma-glutamyl methyl
CC       ester residues. {ECO:0000269|PubMed:18514223}.
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         Evidence={ECO:0000269|PubMed:18514223};
CC   -!- DISRUPTION PHENOTYPE: Mutants show lack of Htr methylation.
CC       {ECO:0000269|PubMed:18514223}.
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DR   EMBL; AM774415; CAP13660.1; -; Genomic_DNA.
DR   RefSeq; WP_012289253.1; NC_010364.1.
DR   AlphaFoldDB; B0R4J5; -.
DR   SMR; B0R4J5; -.
DR   EnsemblBacteria; CAP13660; CAP13660; OE_2406R.
DR   GeneID; 5952759; -.
DR   GeneID; 62886516; -.
DR   KEGG; hsl:OE_2406R; -.
DR   HOGENOM; CLU_025854_1_1_2; -.
DR   OMA; EWQEFVN; -.
DR   PhylomeDB; B0R4J5; -.
DR   Proteomes; UP000001321; 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   1: Evidence at protein level;
KW   Chemotaxis; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..268
FT                   /note="Chemotaxis protein methyltransferase"
FT                   /id="PRO_0000429069"
FT   DOMAIN          1..265
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00051"
FT   BINDING         68
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         70
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         108
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         192..193
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         208..209
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   268 AA;  30533 MW;  546071D347836DB1 CRC64;
     MTDFQTLLEF IETETGFATS YYDESYLDRR VSARMRRRGV EEYAGYLTLL EEDDDDERAE
     LLDTLSVNVT EFFRDEKVWT ALRDVLLELA DTVRSIDIWS AACADGREPY SLAMLALDAG
     LDPRNVSILA TDIDEDALAR ARAGRYESTR TADISDQLGF LDNPQEYVDR EGDRAFVVND
     RVKDLVTFER HDLITGDPKS GFDLVACRNV CIYIDKQYKL PILDTVSKSL REGGHLVLGQ
     TETLPGEVKE RFEAEDPRIR IYSRVADT