CHER_ALKHC
ID CHER_ALKHC Reviewed; 257 AA.
AC Q9KCB8;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Chemotaxis protein methyltransferase;
DE EC=2.1.1.80;
GN Name=cheR; OrderedLocusNames=BH1655;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(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; BA000004; BAB05374.1; -; Genomic_DNA.
DR PIR; G83856; G83856.
DR RefSeq; WP_010897817.1; NC_002570.2.
DR AlphaFoldDB; Q9KCB8; -.
DR SMR; Q9KCB8; -.
DR STRING; 272558.10174272; -.
DR PRIDE; Q9KCB8; -.
DR EnsemblBacteria; BAB05374; BAB05374; BAB05374.
DR KEGG; bha:BH1655; -.
DR eggNOG; COG1352; Bacteria.
DR HOGENOM; CLU_025854_1_1_9; -.
DR OMA; EWQEFVN; -.
DR OrthoDB; 1378151at2; -.
DR Proteomes; UP000001258; Chromosome.
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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..257
FT /note="Chemotaxis protein methyltransferase"
FT /id="PRO_0000176029"
FT DOMAIN 1..257
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 109
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 186..187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 202..203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 257 AA; 30546 MW; F6C9AD28FDADEBF9 CRC64;
MADDYNWFIE QVKERTGIDL NLYKETQMKR RLIALREKRN YQDFRSYFTA MTNDDTLQNE
FLERMTINVS EFFRNRKRWD VLDETIIPQL LKEKKRLKVW SAACSTGEEP YTLAMILQKH
LPLKDVSILA TDIDRAILQQ AKVGYYTERS LKEIPVELKE GFFTKDRAGY YVSNELKQAV
TFKQHNLLAD RFERDCDLIV CRNVLIYFTE EAKRELYHKF SEALRPGGVL FVGSTEQIFE
ASKYGLETNE TFFYRKV