ID S5RZF1_RHIET Unreviewed; 302 AA.
AC S5RZF1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Chemotaxis protein methyltransferase {ECO:0000256|PIRNR:PIRNR000410};
DE EC=2.1.1.80 {ECO:0000256|PIRNR:PIRNR000410};
GN Name=cheR-1 {ECO:0000313|EMBL:AGS20506.1};
GN ORFNames=REMIM1_CH00653 {ECO:0000313|EMBL:AGS20506.1};
OS Rhizobium etli bv. mimosae str. Mim1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=1328306 {ECO:0000313|EMBL:AGS20506.1, ECO:0000313|Proteomes:UP000015261};
RN [1] {ECO:0000313|EMBL:AGS20506.1, ECO:0000313|Proteomes:UP000015261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mim1 {ECO:0000313|EMBL:AGS20506.1,
RC ECO:0000313|Proteomes:UP000015261};
RA Rogel M.A., Bustos P., Santamaria R.I., Gonzalez V., Romero D.,
RA Cevallos M.A., Lozano L., Ormeno-Orrillo E., Martinez-Romero E.;
RT "Genomic basis of Rhizobium etli symbiovar mimosae and its prevalence among
RT Phaseolus vulgaris nodule bacteria.";
RL Submitted (MAY-2013) 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; CP005950; AGS20506.1; -; Genomic_DNA.
DR RefSeq; WP_020920377.1; NC_021905.1.
DR AlphaFoldDB; S5RZF1; -.
DR KEGG; rel:REMIM1_CH00653; -.
DR PATRIC; fig|1328306.3.peg.658; -.
DR HOGENOM; CLU_025854_0_0_5; -.
DR Proteomes; UP000015261; 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 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 17..296
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 222..223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT BINDING 239..240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
SQ SEQUENCE 302 AA; 34272 MW; 47E9946327360CA8 CRC64;
MSAMGAKDQR QGADEVLASG EYPLTRRDLT EIAAMIYSDA GIFLNETKAS LVYSRLSKHI
RNLGLSGFRE YCELVASPAG AAARREMLSH LTTNFTRFFR ENHHFEHLRD HVLPELLQRA
RSGGRVRIWS AASSDGQEPY SIALTVLSLM PNVADYDFKI LATDIDPKIL AIARAGAYDE
SALETVSPAM RKQWFSEVEV QGRRKFQVDD RVKRLITYNE LNLMAQWPFK GKFDVIFCRN
VVIYFDEPTQ MKIWQRFAGL LPEGGHLYIG HSERVSGEAK HVFDNIGITT YRYTTKGLGR
KA
//
