ID A0A974Y5I0_9RHOO Unreviewed; 326 AA.
AC A0A974Y5I0;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 02-APR-2025, entry version 7.
DE RecName: Full=Chemotaxis protein methyltransferase {ECO:0000256|PIRNR:PIRNR000410};
DE EC=2.1.1.80 {ECO:0000256|PIRNR:PIRNR000410};
GN ORFNames=IWH25_08945 {ECO:0000313|EMBL:QRJ65430.1};
OS Azospira restricta.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Rhodocyclales; Rhodocyclaceae; Azospira.
OX NCBI_TaxID=404405 {ECO:0000313|EMBL:QRJ65430.1, ECO:0000313|Proteomes:UP000663444};
RN [1] {ECO:0000313|EMBL:QRJ65430.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 18626 {ECO:0000313|EMBL:QRJ65430.1};
RA Moe W.M.;
RT "Azospira restricta DSM 18626 genome sequence.";
RL Submitted (NOV-2020) 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:0000256|PIRNR:PIRNR000410}.
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:0000256|ARBA:ARBA00001541,
CC ECO:0000256|PIRNR:PIRNR000410};
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DR EMBL; CP064781; QRJ65430.1; -; Genomic_DNA.
DR RefSeq; WP_203388961.1; NZ_CP064781.1.
DR KEGG; ares:IWH25_08945; -.
DR Proteomes; UP000663444; Chromosome.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR050903; Bact_Chemotaxis_MeTrfase.
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 PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF19; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
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; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50123; CHER; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR000410};
KW Reference proteome {ECO:0000313|Proteomes:UP000663444};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR000410};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000410}.
FT DOMAIN 52..324
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..27
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..39
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 192
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 250..251
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 268..269
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
SQ SEQUENCE 326 AA; 36399 MW; 6DA5447202E0D58E CRC64;
MSFDPKRPVP PRAPAAPSSS LRPAAAGRPP PAAPSPSRPA PAGALPFASR DGSLREFEFT
SADFDRVRKL IYQHAGISLS PAKQDMVYSR LARRLRATGK GSFADYLALL ERGDAEEWER
FVNSLTTNLT SFFREPHHFP IFGEHLKKLG GRNPIRVWCC ASSTGEEPYS IAMTVAETFG
GFSTPVSIIA SDLDTNVLAT ADKGVYPIER VERLSPERLK RFFLRGSGAQ EGNVAVRPEL
RRMVQFQRVN LLDPSWPVKG ALDVIFCRNV MIYFDKPTQY RILSRFAPLL QDDGLLFAGH
SESFLHAADL FRSLGKTVYE LSRRRR
//
