ID K4KEH5_SIMAS Unreviewed; 268 AA.
AC K4KEH5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Chemotaxis protein methyltransferase {ECO:0000256|PIRNR:PIRNR000410};
DE EC=2.1.1.80 {ECO:0000256|PIRNR:PIRNR000410};
GN OrderedLocusNames=M5M_00420 {ECO:0000313|EMBL:AFU97321.1};
OS Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Simiduia.
OX NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFU97321.1, ECO:0000313|Proteomes:UP000000466};
RN [1] {ECO:0000313|EMBL:AFU97321.1, ECO:0000313|Proteomes:UP000000466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC {ECO:0000313|Proteomes:UP000000466};
RX PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT bacterium able to degrade a variety of polysaccharides.";
RL Genome Announc. 1:E00039-E00039(2013).
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; CP003746; AFU97321.1; -; Genomic_DNA.
DR AlphaFoldDB; K4KEH5; -.
DR STRING; 1117647.M5M_00420; -.
DR KEGG; saga:M5M_00420; -.
DR eggNOG; COG1352; Bacteria.
DR HOGENOM; CLU_025854_0_0_6; -.
DR Proteomes; UP000000466; Chromosome.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
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; 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:UP000000466};
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 1..268
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 197..198
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 214..215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
SQ SEQUENCE 268 AA; 31225 MW; 3ACBCFE7B6158D5B CRC64;
MYELSAADFR FLCSLVYEHS GIVLGEAKRH MLYRRIMRRI RILKIDSFAG YCNYIRRNAQ
QELPAFINAV TTNLTRFFRE YHHFEYLKQE YLPQLKRAGS GRVRLWSAGC STGEEAYSLA
MCLRSVFADH ELDDKLILAT DLDTEVLDVA SQGCYPMSAV KDIAPAEQAR YFLKDKRNAL
CKVKPEISTL IRFRQLNLLN EWPMRGQFDV IFCRNVLIYF DRETQYQVVS RLAQRLHSGG
LLCLGHSESL DRRVMGLVPV GRTMFRRQ
//
