ID A0A0K8QLH8_9GAMM Unreviewed; 282 AA.
AC A0A0K8QLH8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chemotaxis protein methyltransferase {ECO:0000256|PIRNR:PIRNR000410};
DE EC=2.1.1.80 {ECO:0000256|PIRNR:PIRNR000410};
GN ORFNames=MBSD_2561 {ECO:0000313|EMBL:GAN45959.1}, MBSD_n0566
GN {ECO:0000313|EMBL:GAP65277.1};
OS Mizugakiibacter sediminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Mizugakiibacter.
OX NCBI_TaxID=1475481 {ECO:0000313|EMBL:GAP65277.1};
RN [1] {ECO:0000313|EMBL:GAN45959.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SkMP5 {ECO:0000313|EMBL:GAN45959.1};
RA Watanabe T., Kojima H., Fukui M.;
RT "Draft genome sequence of Mizugakiibacter sediminis skMP5.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAP65277.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SkMP5 {ECO:0000313|EMBL:GAP65277.1};
RA Rikkerink E.H.A., Fineran P.C.;
RT "Complete DNA Sequence of Pseudomonas syringae pv. actinidiae, the Causal
RT Agent of Kiwifruit Canker Disease.";
RL Submitted (AUG-2015) 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; DF952452; GAN45959.1; -; Genomic_DNA.
DR EMBL; DF970156; GAP65277.1; -; Genomic_DNA.
DR RefSeq; WP_062534906.1; NZ_DF970156.1.
DR AlphaFoldDB; A0A0K8QLH8; -.
DR STRING; 1475481.GCA_000953855_00574; -.
DR HOGENOM; CLU_025854_0_0_6; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000253740; Unassembled WGS sequence.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
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; 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:UP000253740};
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 7..282
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 89
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 209..210
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 226..227
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
SQ SEQUENCE 282 AA; 32131 MW; A5564195F3E381BA CRC64;
MAATAFAAEH AYAFTDADFR FLREFVAARC GIALGEHKRQ LVYGRLARRL RALGLGSFAQ
YCELLRREPE RELDALVSAI STNVTAFFRE AHHFEFLAGE LLPRWLTACG GRVRLWSAGC
ATGEEPYTLA MVLAEALERH GAADARILAT DISPQALETA RRGVYRLDRL GNIDAARRRR
WFLRGTGAHD GQAMVHPRLR ELVTFQPLNL LEAWPMRGRF DAIFCRNVVI YFDKPTKERL
FERFADQLAD DGYLFLGHSE SLYGKSERFR LVGRTIYRRV TA
//
