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Database: UniProt
Entry: A0A1G7RBS0_9GAMM
LinkDB: A0A1G7RBS0_9GAMM
Original site: A0A1G7RBS0_9GAMM 
ID   A0A1G7RBS0_9GAMM        Unreviewed;       291 AA.
AC   A0A1G7RBS0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Chemotaxis protein methyltransferase {ECO:0000256|PIRNR:PIRNR000410};
DE            EC=2.1.1.80 {ECO:0000256|PIRNR:PIRNR000410};
GN   ORFNames=SAMN05216571_104175 {ECO:0000313|EMBL:SDG08192.1};
OS   Halomonas taeanensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=284577 {ECO:0000313|EMBL:SDG08192.1, ECO:0000313|Proteomes:UP000198641};
RN   [1] {ECO:0000313|EMBL:SDG08192.1, ECO:0000313|Proteomes:UP000198641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH539 {ECO:0000313|EMBL:SDG08192.1,
RC   ECO:0000313|Proteomes:UP000198641};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNCI01000004; SDG08192.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7RBS0; -.
DR   STRING; 284577.SAMN05216571_104175; -.
DR   Proteomes; UP000198641; 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:UP000198641};
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          19..290
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   BINDING         96
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         98
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         102
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         133
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         158
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         216..217
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
FT   BINDING         234..235
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000410-1"
SQ   SEQUENCE   291 AA;  33065 MW;  DC1C2E3B83694095 CRC64;
     MNSHVSHEAA GQGGWSASMA ERDLVLTEKD FTRIRELIYQ RAGIVLAEHK REMVYSRLAK
     RLRHHGLTHF SDYLARLERQ PEAREWEAFT NALTTNLTAF FREAHHFPLL SKHVAERRDT
     VRVWSAAAST GEEPYSIAMT LREALGSRAE QCKVVATDID SDALNRARDG IYAMDQVAKL
     DEGRIKRFFQ KGSGRRAGFA RVRPEVASMV EFKSLNLLAP GWPIEGPFDA IFCRNVMIYF
     DKTTQAKILQ RFAPLLKPDG LLFAGHSENF SYISDAFRLR GQTVYTLSPR A
//
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